Jacalin-like lectin domain

{{Infobox protein family

| Symbol = Jacalin

| Name = Jacalin-like lectin domain

| image = PDB 1c3n EBI.jpg

| width =

| caption = crystal structure of helianthus tuberosus lectin complexed to man(1-2)man

| Pfam = PF01419

| Pfam_clan =

| InterPro = IPR001229

| SMART =

| PROSITE =

| MEROPS =

| SCOP = 1jac

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

In molecular biology, the jacalin-like lectin domain is a mannose-binding lectin domain with a beta-prism fold consisting of three 4-stranded beta-sheets, with an internal pseudo 3-fold symmetry. Some lectins in this group stimulate distinct T- and B-cell functions, such as Jacalin, which binds to the T-antigen and acts as an agglutinin. This domain is found in 1 to 6 copies in lectins. The domain is also found in the salt-stress induced protein from rice and an animal prostatic spermine-binding protein.

Database of jacalin like lectins and structure function relations.Raval et al, "A database analysis of jacalin-like lectins: sequence–structure–function relationships" Glycobiology vol. 14 no. 12 pp. 1247–1263, 2004 http://glycob.oxfordjournals.org/content/14/12/1247.full.pdf Proteins containing this domain include:

  • Jacalin, a tetrameric plant seed lectin and agglutinin from Artocarpus heterophyllus (jackfruit), which is specific for galactose.{{cite journal |vauthors=Jeyaprakash AA, Geetha Rani P, Banuprakash Reddy G, Banumathi S, Betzel C, Sekar K, Surolia A, Vijayan M | title = Crystal structure of the jacalin-T-antigen complex and a comparative study of lectin-T-antigen complexes | journal = J. Mol. Biol. | volume = 321 | issue = 4 | pages = 637–45 |date=August 2002 | pmid = 12206779 | doi = 10.1016/S0022-2836(02)00674-5| citeseerx = 10.1.1.532.2424 }}
  • Artocarpin, a tetrameric plant seed lectin from A. heterophyllus.{{cite journal |vauthors=Jeyaprakash AA, Srivastav A, Surolia A, Vijayan M | title = Structural basis for the carbohydrate specificities of artocarpin: variation in the length of a loop as a strategy for generating ligand specificity | journal = J. Mol. Biol. | volume = 338 | issue = 4 | pages = 757–70 |date=May 2004 | pmid = 15099743 | doi = 10.1016/j.jmb.2004.03.040 | citeseerx = 10.1.1.530.4331 }}
  • Lectin MPA, a tetrameric plant seed lectin and agglutinin from Maclura pomifera (Osage orange).{{cite journal |vauthors=Lee X, Thompson A, Zhang Z, Ton-that H, Biesterfeldt J, Ogata C, Xu L, Johnston RA, Young NM | title = Structure of the complex of Maclura pomifera agglutinin and the T-antigen disaccharide, Galbeta1,3GalNAc | journal = J. Biol. Chem. | volume = 273 | issue = 11 | pages = 6312–8 |date=March 1998 | pmid = 9497359 | doi = 10.1074/jbc.273.11.6312| doi-access = free }}
  • Heltuba lectin, a plant seed lectin and agglutinin from Helianthus tuberosus (Jerusalem artichoke).{{cite journal |vauthors=Bourne Y, Zamboni V, Barre A, Peumans WJ, Van Damme EJ, Rouge P | title = Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins | journal = Structure | volume = 7 | issue = 12 | pages = 1473–82 |date=December 1999 | pmid = 10647178 | doi = 10.1016/s0969-2126(00)88338-0| doi-access = free }}
  • Agglutinin from Calystegia sepium (Hedge bindweed).{{cite journal |vauthors=Bourne Y, Roig-Zamboni V, Barre A, Peumans WJ, Astoul CH, Van Damme EJ, Rouge P | title = The crystal structure of the Calystegia sepium agglutinin reveals a novel quaternary arrangement of lectin subunits with a beta-prism fold | journal = J. Biol. Chem. | volume = 279 | issue = 1 | pages = 527–33 |date=January 2004 | pmid = 14561768 | doi = 10.1074/jbc.M308218200 | doi-access = free }}
  • Griffithsin, an anti-viral lectin from red algae (Griffithsia species).{{cite journal |vauthors=Ziolkowska NE, O'Keefe BR, Mori T, Zhu C, Giomarelli B, Vojdani F, Palmer KE, McMahon JB, Wlodawer A | title = Domain-swapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding | journal = Structure | volume = 14 | issue = 7 | pages = 1127–35 |date=July 2006 | pmid = 16843894 | doi = 10.1016/j.str.2006.05.017 | pmc = 7126681 }}

References

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{{InterPro content|IPR001229}}

Category:Protein domains