beta-2 adrenergic receptor

The {{gene|ADRB2}} gene is intronless. Different polymorphic forms, point mutations, and/or downregulation of this gene are associated with nocturnal asthma, obesity and type 2 diabetes.{{cite web | title = Entrez Gene: ADRB2 adrenergic, beta-2-, receptor, surface| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=154}}

The 3D crystallographic structure (see figure and links to the right) of the β₂-adrenergic receptor has been determined{{cite journal |vauthors=Cherezov V, Rosenbaum DM, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Kuhn P, Weis WI, Kobilka BK, Stevens RC | title = High-resolution crystal structure of an engineered human β₂-adrenergic G protein-coupled receptor | journal = Science | volume = 318 | issue = 5854 | pages = 1258–65 | year = 2007 | pmid = 17962520 | doi = 10.1126/science.1150577 | pmc=2583103| bibcode = 2007Sci...318.1258C }}{{cite journal |vauthors=Rosenbaum DM, Cherezov V, Hanson MA, Rasmussen SG, Thian FS, Kobilka TS, Choi HJ, Yao XJ, Weis WI, Stevens RC, Kobilka BK | title = GPCR engineering yields high-resolution structural insights into β₂-adrenergic receptor function | journal = Science | volume = 318 | issue = 5854 | pages = 1266–73 | year = 2007 | pmid = 17962519 | doi = 10.1126/science.1150609 | bibcode = 2007Sci...318.1266R | s2cid = 1559802 | doi-access = free }}{{cite journal | vauthors = Rasmussen SG, Choi HJ, Rosenbaum DM, Kobilka TS, Thian FS, Edwards PC, Burghammer M, Ratnala VR, Sanishvili R, Fischetti RF, Schertler GF, Weis WI, Kobilka BK | title = Crystal structure of the human beta2 adrenergic G-protein-coupled receptor | journal = Nature | volume = 450 | issue = 7168 | pages = 383–7 | date = Nov 2007 | pmid = 17952055 | doi = 10.1038/nature06325 | bibcode = 2007Natur.450..383R | s2cid = 4407117 }} by making a fusion protein with lysozyme to increase the hydrophilic surface area of the protein for crystal contacts. An alternative method, involving production of a fusion protein with an agonist, supported lipid-bilayer co-crystallization and generation of a 3.5 Å resolution structure.{{cite journal| vauthors = Liszewski K |date=1 October 2015|title=Dissecting the Structure of Membrane Proteins|url=http://www.genengnews.com/gen-articles/dissecting-the-structure-of-membrane-proteins/5583/|journal=Genetic Engineering & Biotechnology News|volume=35|issue=17|page=16|type=paper|doi=10.1089/gen.35.07.09|url-access=subscription}}{{subscription required}}

The crystal structure of the β₂Adrenergic Receptor-G_s protein complex was solved in 2011. The largest conformational changes in the β2AR include a 14 Å outward movement at the cytoplasmic end of transmembrane segment 6 (TM6) and an alpha helical extension of the cytoplasmic end of TM5.{{cite journal | vauthors = Rasmussen SG, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, Mathiesen JM, Shah ST, Lyons JA, Caffrey M, Gellman SH, Steyaert J, Skiniotis G, Weis WI, Sunahara RK, Kobilka BK | display-authors = 6 | title = Crystal structure of the β2 adrenergic receptor-Gs protein complex | journal = Nature | volume = 477 | issue = 7366 | pages = 549–55 | date = July 2011 | pmid = 21772288 | pmc = 3184188 | doi = 10.1038/nature10361 | bibcode = 2011Natur.477..549R }}

This receptor is directly associated with one of its ultimate effectors, the class C L-type calcium channel Ca_V1.2.{{citation needed|date=September 2023}} This receptor-channel complex is coupled to the G_s G protein, which activates adenylyl cyclase, catalysing the formation of cyclic adenosine monophosphate (cAMP) which then activates protein kinase A, and counterbalancing phosphatase PP2A. Protein kinase A then goes on to phosphorylate (and thus inactivate) myosin light-chain kinase, which causes smooth muscle relaxation, accounting for the vasodilatory effects of beta 2 stimulation. The assembly of the signaling complex provides a mechanism that ensures specific and rapid signaling. A two-state biophysical and molecular model has been proposed to account for the pH and REDOX sensitivity of this and other GPCRs.{{cite journal | vauthors = Rubenstein LA, Zauhar RJ, Lanzara RG | title = Molecular dynamics of a biophysical model for beta2-adrenergic and G protein-coupled receptor activation | journal = Journal of Molecular Graphics & Modelling | volume = 25 | issue = 4 | pages = 396–409 | date = Dec 2006 | pmid = 16574446 | doi = 10.1016/j.jmgm.2006.02.008 }}

Beta-2 adrenergic receptors have also been found to couple with G_i, possibly providing a mechanism by which response to ligand is highly localized within cells. In contrast, Beta-1 adrenergic receptors are coupled only to G_s, and stimulation of these results in a more diffuse cellular response.{{cite journal | vauthors = Chen-Izu Y, Xiao RP, Izu LT, Cheng H, Kuschel M, Spurgeon H, Lakatta EG | title = G(i)-dependent localization of beta(2)-adrenergic receptor signaling to L-type Ca(2+) channels | journal = Biophysical Journal | volume = 79 | issue = 5 | pages = 2547–56 | date = Nov 2000 | pmid = 11053129 | pmc = 1301137 | doi = 10.1016/S0006-3495(00)76495-2 | bibcode = 2000BpJ....79.2547C }} This appears to be mediated by cAMP induced PKA phosphorylation of the receptor.{{cite journal | vauthors = Zamah AM, Delahunty M, Luttrell LM, Lefkowitz RJ | title = Protein kinase A-mediated phosphorylation of the beta 2-adrenergic receptor regulates its coupling to Gs and Gi. Demonstration in a reconstituted system | journal = The Journal of Biological Chemistry | volume = 277 | issue = 34 | pages = 31249–56 | date = Aug 2002 | pmid = 12063255 | doi = 10.1074/jbc.M202753200 | doi-access = free }}

Interestingly, Beta-2 adrenergic receptor was observed to localize exclusively to the T-tubular network of adult cardiomyocytes, as opposed to Beta-1 adrenergic receptor, which is observed also on the outer plasma membrane of the cell {{cite journal | vauthors = Bathe-Peters M, Gmach P, Boltz HH, Einsiedel J, Gotthardt M, Hübner H, Gmeiner P, Lohse MJ, Annibale P | display-authors = 6 | title = Visualization of β-adrenergic receptor dynamics and differential localization in cardiomyocytes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 118 | issue = 23 | page = e2101119118 | date = June 2021 | pmid = 34088840 | doi = 10.1073/pnas.2101119118|issn=0027-8424 | pmc = 8201832 | doi-access = free | bibcode = 2021PNAS..11801119B }}

Activation of the β₂ adrenoreceptor with long-acting agents such as oral clenbuterol and intravenously-infused albuterol results in skeletomuscular hypertrophy and anabolism.{{cite journal | vauthors = Choo JJ, Horan MA, Little RA, Rothwell NJ | title = Anabolic effects of clenbuterol on skeletal muscle are mediated by beta 2-adrenoceptor activation | journal = The American Journal of Physiology | volume = 263 | issue = 1 Pt 1 | pages = E50-6 | date = July 1992 | pmid = 1322047 | doi = 10.1152/ajpendo.1992.263.1.E50 }}{{cite journal | vauthors = Kamalakkannan G, Petrilli CM, George I, LaManca J, McLaughlin BT, Shane E, Mancini DM, Maybaum S | display-authors = 6 | title = Clenbuterol increases lean muscle mass but not endurance in patients with chronic heart failure | journal = The Journal of Heart and Lung Transplantation | volume = 27 | issue = 4 | pages = 457–61 | date = April 2008 | pmid = 18374884 | doi = 10.1016/j.healun.2008.01.013 }} The comprehensive anabolic, lipolytic, and ergogenic effects of long-acting β₂ agonists such as clenbuterol render them frequent targets as performance-enhancing drugs in athletes.{{cite journal | vauthors = Davis E, Loiacono R, Summers RJ | title = The rush to adrenaline: drugs in sport acting on the beta-adrenergic system | journal = British Journal of Pharmacology | volume = 154 | issue = 3 | pages = 584–97 | date = June 2008 | pmid = 18500380 | pmc = 2439523 | doi = 10.1038/bjp.2008.164 }} Consequently, such agents are monitored for and generally banned by WADA (World Anti-Doping Agency) with limited permissible usage under therapeutic exemptions; clenbuterol and other β₂ adrenergic agents remain banned not as a beta-agonist, but rather an anabolic agent. These effects are largely attractive within agricultural contexts insofar that β₂ adrenergic agents have seen notable extra-label usage in food-producing animals and livestock. While many countries including the United States have prohibited extra-label usage in food-producing livestock, the practice is still observed in many countries.{{cite web |title=Clenbuterol |url=https://www.deadiversion.usdoj.gov/drug_chem_info/clenbuterol.pdf |website=Drug and Chemical Evaluation Section |publisher=Drug Enforcement Agency |access-date=15 November 2021}}{{cite web |title=Food and Drugs - ANIMAL DRUGS, FEEDS, AND RELATED PRODUCTS |url=https://www.accessdata.fda.gov/scripts/cdrh/cfdocs/cfcfr/cfrsearch.cfm?fr=530.41 |archive-url=https://web.archive.org/web/20030917005926/http://www.accessdata.fda.gov/scripts/cdrh/cfdocs/cfcfr/CFRSearch.cfm?FR=530.41 |url-status=dead |archive-date=September 17, 2003 |publisher=U.S. Food and Drug Administration |access-date=15 November 2021}}

• Heart muscle contraction
• Increase cardiac output (minor degree compared to β₁).
• Increases heart rate in sinoatrial node (SA node) (chronotropic effect).
• Increases atrial cardiac muscle contractility. (inotropic effect).
• Increases contractility and automaticity of ventricular cardiac muscle.
• Dilate hepatic artery.
• Dilate arterioles to skeletal muscle.

In the normal eye, beta-2 stimulation by salbutamol increases intraocular pressure via net:

• Increase in production of aqueous humour by the ciliary process,
• Subsequent increased pressure-dependent uveoscleral outflow of humour, despite reduced drainage of humour via the Canal of Schlemm.

In glaucoma, drainage is reduced (open-angle glaucoma) or blocked completely (closed-angle glaucoma). In such cases, beta-2 stimulation with its consequent increase in humour production is highly contra-indicated, and conversely, a topical beta-2 antagonist such as timolol may be employed.

• Glycogenolysis and gluconeogenesis in liver.
• Glycogenolysis and lactate release in skeletal muscle.
• Contract sphincters of Gastrointestinal tract.
• Thickened secretions from salivary glands.
• Insulin and glucagon secretion from pancreas.

• Inhibit histamine-release from mast cells.
• Increase protein content of secretions from lacrimal glands.
• Receptor also present in cerebellum.
• Bronchiole dilation (targeted while treating asthma attacks)
• Involved in brain - immune - communication {{cite journal | vauthors = Elenkov IJ, Wilder RL, Chrousos GP, Vizi ES | title = The sympathetic nerve--an integrative interface between two supersystems: the brain and the immune system | journal = Pharmacological Reviews | volume = 52 | issue = 4 | pages = 595–638 | date = Dec 2000 | pmid = 11121511 }}

{{Infobox GPCR

| name = Beta-2 adrenergic receptor

| signal transduction = Primary: G_s
Secondary: G_i/o

| primary endogenous agonists = epinephrine, norepinephrine

| agonists = isoprenaline, salbutamol, salmeterol, others

| antagonists = carvedilol, propranolol, labetalol, others

| inverse agonists = N/A

| PAMs = Zn²⁺ (low concentrations)

| NAMs = Zn²⁺ (high concentrations)

| IUPHAR Target ID = 29

| DrugBank Polypeptides ID = P07550

| HMDB Protein ID = HMDBP01634

}}

{{Main|Beta2-adrenergic agonist|l1=Beta₂-adrenergic agonist}}

• Short-acting β₂ agonists (SABA)
• bitolterol
• fenoterol
• hexoprenaline
• isoprenaline (INN) or isoproterenol (USAN)
• levosalbutamol (INN) or levalbuterol (USAN)
• orciprenaline (INN) or metaproterenol (USAN)
• pirbuterol
• procaterol
• salbutamol (INN) or albuterol (USAN)
• terbutaline
• Long-acting β₂ agonists (LABA)
• arformoterol (some consider it to be an ultra-LABA){{cite journal | vauthors = Matera MG, Cazzola M | title = ultra-long-acting beta2-adrenoceptor agonists: an emerging therapeutic option for asthma and COPD? | journal = Drugs | volume = 67 | issue = 4 | pages = 503–15 | date = 2007 | pmid = 17352511 | doi = 10.2165/00003495-200767040-00002 | s2cid = 46976912 }}
• bambuterol
• clenbuterol
• formoterol
• salmeterol
• Ultra-long-acting β₂ agonists (ultra-LABA)
• carmoterol
• indacaterol
• milveterol (GSK 159797)
• olodaterol
• vilanterol (GSK 642444)

• Short-acting β₂ agonists (SABA)
• fenoterol
• hexoprenaline
• isoxsuprine
• ritodrine
• salbutamol (INN) or albuterol (USAN)
• terbutaline

• zilpaterol

(Beta blockers)

• butoxamine*
• First generation (non-selective) β-blockers
• ICI-118,551*
• Propranolol

* denotes selective antagonist to the receptor.

• compound-6FA,{{cite journal | vauthors = Liu X, Masoudi A, Kahsai AW, Huang LY, Pani B, Staus DP, Shim PJ, Hirata K, Simhal RK, Schwalb AM, Rambarat PK, Ahn S, Lefkowitz RJ, Kobilka B | display-authors = 6 | title = Mechanism of β₂AR regulation by an intracellular positive allosteric modulator | journal = Science | volume = 364 | issue = 6447 | pages = 1283–1287 | date = June 2019 | pmid = 31249059 | pmc = 6705129 | doi = 10.1126/science.aaw8981 | bibcode = 2019Sci...364.1283L }} PAM at intracellular binding site
• Cellular swelling {{cite journal | vauthors = Sirbu A, Bathe-Peters M, Kumar J, Inoue A, Lohse MJ, Annibale P | title = Cell swelling enhances ligand-driven β-adrenergic signaling | journal = Nature Communications | volume = 15 | issue = 1 | pages = 1-12 | date = August 2024 | doi = 10.1038/s41467-024-52191-y| pmc = 11379887 }}

Beta-2 adrenergic receptor has been shown to interact with:

{{div col|colwidth=20em}}

• AKAP12,{{cite journal | vauthors = Fan G, Shumay E, Wang H, Malbon CC | title = The scaffold protein gravin (cAMP-dependent protein kinase-anchoring protein 250) binds the beta 2-adrenergic receptor via the receptor cytoplasmic Arg-329 to Leu-413 domain and provides a mobile scaffold during desensitization | journal = The Journal of Biological Chemistry | volume = 276 | issue = 26 | pages = 24005–14 | date = Jun 2001 | pmid = 11309381 | doi = 10.1074/jbc.M011199200 | doi-access = free }}{{cite journal | vauthors = Shih M, Lin F, Scott JD, Wang HY, Malbon CC | title = Dynamic complexes of beta2-adrenergic receptors with protein kinases and phosphatases and the role of gravin | journal = The Journal of Biological Chemistry | volume = 274 | issue = 3 | pages = 1588–95 | date = Jan 1999 | pmid = 9880537 | doi = 10.1074/jbc.274.3.1588 | doi-access = free }}
• OPRD1,{{cite journal | vauthors = McVey M, Ramsay D, Kellett E, Rees S, Wilson S, Pope AJ, Milligan G | title = Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta -opioid receptor displays constitutive oligomerization at the cell surface, which is not regulated by receptor occupancy | journal = The Journal of Biological Chemistry | volume = 276 | issue = 17 | pages = 14092–9 | date = Apr 2001 | pmid = 11278447 | doi = 10.1074/jbc.M008902200 | doi-access = free }}
• Grb2,{{cite journal | vauthors = Karoor V, Wang L, Wang HY, Malbon CC | title = Insulin stimulates sequestration of beta-adrenergic receptors and enhanced association of beta-adrenergic receptors with Grb2 via tyrosine 350 | journal = The Journal of Biological Chemistry | volume = 273 | issue = 49 | pages = 33035–41 | date = Dec 1998 | pmid = 9830057 | doi = 10.1074/jbc.273.49.33035 | doi-access = free }}
• SNX27{{cite journal | vauthors = Temkin P, Lauffer B, Jäger S, Cimermancic P, Krogan NJ, von Zastrow M | title = SNX27 mediates retromer tubule entry and endosome-to-plasma membrane trafficking of signalling receptors | journal = Nature Cell Biology | volume = 13 | issue = 6 | pages = 715–21 | date = Jun 2011 | pmid = 21602791 | pmc = 3113693 | doi = 10.1038/ncb2252 }} and
• SLC9A3R1.{{cite journal | vauthors = Karthikeyan S, Leung T, Ladias JA | title = Structural determinants of the Na+/H+ exchanger regulatory factor interaction with the beta 2 adrenergic and platelet-derived growth factor receptors | journal = The Journal of Biological Chemistry | volume = 277 | issue = 21 | pages = 18973–8 | date = May 2002 | pmid = 11882663 | doi = 10.1074/jbc.M201507200 | doi-access = free }}{{cite journal | vauthors = Hall RA, Ostedgaard LS, Premont RT, Blitzer JT, Rahman N, Welsh MJ, Lefkowitz RJ | title = A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 95 | issue = 15 | pages = 8496–501 | date = Jul 1998 | pmid = 9671706 | pmc = 21104 | doi = 10.1073/pnas.95.15.8496 |bibcode = 1998PNAS...95.8496H | doi-access = free }}{{cite journal | vauthors = Hall RA, Premont RT, Chow CW, Blitzer JT, Pitcher JA, Claing A, Stoffel RH, Barak LS, Shenolikar S, Weinman EJ, Grinstein S, Lefkowitz RJ | title = The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange | journal = Nature | volume = 392 | issue = 6676 | pages = 626–30 | date = Apr 1998 | pmid = 9560162 | doi = 10.1038/33458 |bibcode = 1998Natur.392..626H | s2cid = 4422540 }}

{{Div col end}}

• Other adrenergic receptors
• Alpha-1 adrenergic receptor
• Alpha-2 adrenergic receptor
• Beta-1 adrenergic receptor
• Beta-3 adrenergic receptor
• Discovery and development of beta2 agonists

{{Reflist|32em}}

{{refbegin|32em}}

• {{cite journal | vauthors = Frielle T, Caron MG, Lefkowitz RJ | title = Properties of the beta 1- and beta 2-adrenergic receptor subtypes revealed by molecular cloning | journal = Clinical Chemistry | volume = 35 | issue = 5 | pages = 721–5 | date = May 1989 | pmid = 2541947 | doi = 10.1093/clinchem/35.5.721| doi-access = free }}
• {{cite journal | vauthors = Taylor DR, Kennedy MA | title = Genetic variation of the beta(2)-adrenoceptor: its functional and clinical importance in bronchial asthma | journal = American Journal of Pharmacogenomics | volume = 1 | issue = 3 | pages = 165–74 | year = 2002 | pmid = 12083965 | doi = 10.2165/00129785-200101030-00002 | s2cid = 116089602 }}
• {{cite book | vauthors = Thibonnier M, Coles P, Thibonnier A, Shoham M | chapter = Chapter 14 Molecular pharmacology and modeling of vasopressin receptors | title = Vasopressin and Oxytocin: From Genes to Clinical Applications | series = Progress in Brain Research | volume = 139 | pages = 179–96 | year = 2002 | pmid = 12436935 | doi = 10.1016/S0079-6123(02)39016-2 | isbn = 9780444509826 }}
• {{cite journal | vauthors = Ge D, Huang J, He J, Li B, Duan X, Chen R, Gu D | title = beta2-Adrenergic receptor gene variations associated with stage-2 hypertension in northern Han Chinese | journal = Annals of Human Genetics | volume = 69 | issue = Pt 1 | pages = 36–44 | date = Jan 2005 | pmid = 15638826 | doi = 10.1046/j.1529-8817.2003.00093.x | s2cid = 6485276 | doi-access = free }}
• {{cite journal | vauthors = Muszkat M | title = Interethnic differences in drug response: the contribution of genetic variability in beta adrenergic receptor and cytochrome P4502C9 | journal = Clinical Pharmacology and Therapeutics | volume = 82 | issue = 2 | pages = 215–8 | date = Aug 2007 | pmid = 17329986 | doi = 10.1038/sj.clpt.6100142 | s2cid = 10381767 }}
• {{cite journal | vauthors = von Zastrow M, Kobilka BK | title = Ligand-regulated internalization and recycling of human beta 2-adrenergic receptors between the plasma membrane and endosomes containing transferrin receptors | journal = The Journal of Biological Chemistry | volume = 267 | issue = 5 | pages = 3530–8 | date = Feb 1992 | doi = 10.1016/S0021-9258(19)50762-1 | pmid = 1371121 | doi-access = free }}
• {{cite journal | vauthors = Gope R, Gope ML, Thorson A, Christensen M, Smyrk T, Chun M, Alvarez L, Wildrick DM, Boman BM | title = Genetic changes at the beta-2-adrenergic receptor locus on chromosome 5 in human colorectal carcinomas | journal = Anticancer Research | volume = 11 | issue = 6 | pages = 2047–50 | year = 1992 | pmid = 1663718 }}
• {{cite journal | vauthors = Bouvier M, Guilbault N, Bonin H | title = Phorbol-ester-induced phosphorylation of the beta 2-adrenergic receptor decreases its coupling to Gs | journal = FEBS Letters | volume = 279 | issue = 2 | pages = 243–8 | date = Feb 1991 | pmid = 1848190 | doi = 10.1016/0014-5793(91)80159-Z | s2cid = 28959833 | doi-access = free | bibcode = 1991FEBSL.279..243B }}
• {{cite journal | vauthors = Yang-Feng TL, Xue FY, Zhong WW, Cotecchia S, Frielle T, Caron MG, Lefkowitz RJ, Francke U | title = Chromosomal organization of adrenergic receptor genes | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 87 | issue = 4 | pages = 1516–20 | date = Feb 1990 | pmid = 2154750 | pmc = 53506 | doi = 10.1073/pnas.87.4.1516 | bibcode = 1990PNAS...87.1516Y | doi-access = free }}
• {{cite journal | vauthors = Hui KK, Yu JL | title = Effects of protein kinase inhibitor, 1-(5-isoquinolinylsulfonyl)-2-methylpiperazine, on beta-2 adrenergic receptor activation and desensitization in intact human lymphocytes | journal = The Journal of Pharmacology and Experimental Therapeutics | volume = 249 | issue = 2 | pages = 492–8 | date = May 1989 | pmid = 2470898 }}
• {{cite journal | vauthors = Hen R, Axel R, Obici S | title = Activation of the beta 2-adrenergic receptor promotes growth and differentiation in thyroid cells | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 12 | pages = 4785–8 | date = Jun 1989 | pmid = 2471981 | pmc = 287358 | doi = 10.1073/pnas.86.12.4785 | bibcode = 1989PNAS...86.4785H | doi-access = free }}
• {{cite journal | vauthors = O'Dowd BF, Hnatowich M, Caron MG, Lefkowitz RJ, Bouvier M | title = Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor | journal = The Journal of Biological Chemistry | volume = 264 | issue = 13 | pages = 7564–9 | date = May 1989 | doi = 10.1016/S0021-9258(18)83271-9 | pmid = 2540197 | doi-access = free }}
• {{cite journal | vauthors = Bristow MR, Hershberger RE, Port JD, Minobe W, Rasmussen R | title = Beta 1- and beta 2-adrenergic receptor-mediated adenylate cyclase stimulation in nonfailing and failing human ventricular myocardium | journal = Molecular Pharmacology | volume = 35 | issue = 3 | pages = 295–303 | date = Mar 1989 | pmid = 2564629 }}
• {{cite journal | vauthors = Emorine LJ, Marullo S, Delavier-Klutchko C, Kaveri SV, Durieu-Trautmann O, Strosberg AD | title = Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 20 | pages = 6995–9 | date = Oct 1987 | pmid = 2823249 | pmc = 299215 | doi = 10.1073/pnas.84.20.6995 | bibcode = 1987PNAS...84.6995E | doi-access = free }}
• {{cite journal | vauthors = Chung FZ, Wang CD, Potter PC, Venter JC, Fraser CM | title = Site-directed mutagenesis and continuous expression of human beta-adrenergic receptors. Identification of a conserved aspartate residue involved in agonist binding and receptor activation | journal = The Journal of Biological Chemistry | volume = 263 | issue = 9 | pages = 4052–5 | date = Mar 1988 | doi = 10.1016/S0021-9258(18)68888-X | pmid = 2831218 | doi-access = free }}
• {{cite journal | vauthors = Yang SD, Fong YL, Benovic JL, Sibley DR, Caron MG, Lefkowitz RJ | title = Dephosphorylation of the beta 2-adrenergic receptor and rhodopsin by latent phosphatase 2 | journal = The Journal of Biological Chemistry | volume = 263 | issue = 18 | pages = 8856–8 | date = Jun 1988 | doi = 10.1016/S0021-9258(18)68386-3 | pmid = 2837466 | doi-access = free }}
• {{cite journal | vauthors = Kobilka BK, Dixon RA, Frielle T, Dohlman HG, Bolanowski MA, Sigal IS, Yang-Feng TL, Francke U, Caron MG, Lefkowitz RJ | title = cDNA for the human beta 2-adrenergic receptor: a protein with multiple membrane-spanning domains and encoded by a gene whose chromosomal location is shared with that of the receptor for platelet-derived growth factor | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 84 | issue = 1 | pages = 46–50 | date = Jan 1987 | pmid = 3025863 | pmc = 304138 | doi = 10.1073/pnas.84.1.46 | bibcode = 1987PNAS...84...46K | doi-access = free }}
• {{cite journal | vauthors = Chung FZ, Lentes KU, Gocayne J, Fitzgerald M, Robinson D, Kerlavage AR, Fraser CM, Venter JC | title = Cloning and sequence analysis of the human brain beta-adrenergic receptor. Evolutionary relationship to rodent and avian beta-receptors and porcine muscarinic receptors | journal = FEBS Letters | volume = 211 | issue = 2 | pages = 200–6 | date = Jan 1987 | pmid = 3026848 | doi = 10.1016/0014-5793(87)81436-9 | s2cid = 221452296 | doi-access = | bibcode = 1987FEBSL.211..200C }}

{{refend}}

• {{cite web | url = http://www.iuphar-db.org/GPCR/ReceptorDisplayForward?receptorID=2189 | title = β₂-adrenoceptor | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | access-date = 2008-11-25 | archive-date = 2015-01-12 | archive-url = https://web.archive.org/web/20150112084733/http://www.iuphar-db.org/GPCR/ReceptorDisplayForward?receptorID=2189 | url-status = dead }}
• {{UCSC gene info|ADRB2}}
• {{PDBe-KB2|P07550| Beta-2 adrenergic receptor}}

{{G protein-coupled receptors|g1}}

Category:Adrenergic receptors