Hexon protein

{{distinguish||text=exon, a part of a gene, or axon, the projection of a neuron}}

{{Infobox protein family

| Symbol = Adeno_hexon

| Name = Adeno_hexon

| image = PDB 1p2z EBI.jpg

| width =

| caption = refinement of adenovirus type 2 hexon with cns

| Pfam = PF01065

| Pfam_clan =

| InterPro = IPR016107

| SMART =

| PROSITE =

| MEROPS =

| SCOP = 1dhx

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

{{Infobox protein family

| Symbol = Adeno_hexon_C

| Name = Adeno_hexon_C

| image = PDB 2bvi EBI.jpg

| width =

| caption = the quasi-atomic model of human adenovirus type 5 capsid (part 2)

| Pfam = PF03678

| Pfam_clan =

| InterPro = IPR016108

| SMART =

| PROSITE =

| MEROPS =

| SCOP = 1dhx

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

In molecular biology, the hexon protein is a major coat protein found in adenoviruses. Hexon coat proteins are synthesised during late infection and form homo-trimers. The 240 copies of the hexon trimer that are produced are organised so that 12 lie on each of the 20 facets. The central 9 hexons in a facet are cemented together by 12 copies of polypeptide IX. The penton complex, formed by the peripentonal hexons and penton base (holding in place a fibre), lie at each of the 12 vertices.{{cite journal | vauthors = Athappilly FK, Murali R, Rux JJ, Cai Z, Burnett RM | title = The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution | journal = Journal of Molecular Biology | volume = 242 | issue = 4 | pages = 430–55 | date = September 1994 | pmid = 7932702 | doi = 10.1006/jmbi.1994.1593 | doi-access = free }} The hexon coat protein is a duplication consisting of two domains with a similar fold packed together like the nucleoplasmin subunits. Within a hexon trimer, the domains are arranged around a pseudo 6-fold axis. The domains have a beta-sandwich structure consisting of 8 strands in two sheets with a jelly-roll topology; each domain is heavily decorated with many insertions.{{cite journal | vauthors = Rux JJ, Kuser PR, Burnett RM | title = Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution x-ray crystallographic, molecular modeling, and sequence-based methods | journal = Journal of Virology | volume = 77 | issue = 17 | pages = 9553–66 | date = September 2003 | pmid = 12915569 | pmc = 187380 | doi = 10.1128/jvi.77.17.9553-9566.2003 }} Some hexon proteins contain a distinct C-terminal domain.

Hexon directly recruits the cellular motor protein dynein in a pH-dependent manner.{{cite journal | vauthors = Bremner KH, Scherer J, Yi J, Vershinin M, Gross SP, Vallee RB | title = Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit | language = English | journal = Cell Host & Microbe | volume = 6 | issue = 6 | pages = 523–35 | date = December 2009 | pmid = 20006841 | pmc = 2810746 | doi = 10.1016/j.chom.2009.11.006 }} The dynein-regulatory protein, dynactin, was found to play a clear role in regulating the dynein-adenovirus complex transport to the nucleus.

References

{{reflist}}

{{InterPro content|IPR016107}}

Category:Protein domains