Biology:Hexon protein
| Adeno_hexon | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 refinement of adenovirus type 2 hexon with cns | |||||||||
| Identifiers | |||||||||
| Symbol | Adeno_hexon | ||||||||
| Pfam | PF01065 | ||||||||
| InterPro | IPR016107 | ||||||||
| SCOP2 | 1dhx / SCOPe / SUPFAM | ||||||||
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| Adeno_hexon_C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 the quasi-atomic model of human adenovirus type 5 capsid (part 2) | |||||||||
| Identifiers | |||||||||
| Symbol | Adeno_hexon_C | ||||||||
| Pfam | PF03678 | ||||||||
| InterPro | IPR016108 | ||||||||
| SCOP2 | 1dhx / SCOPe / SUPFAM | ||||||||
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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.[1] 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.[2] Some hexon proteins contain a distinct C-terminal domain.
Hexon directly recruits the cellular motor protein dynein in a pH-dependent manner.[3] The dynein-regulatory protein, dynactin, was found to play a clear role in regulating the dynein-adenovirus complex transport to the nucleus.
References
- ↑ "The refined crystal structure of hexon, the major coat protein of adenovirus type 2, at 2.9 A resolution". Journal of Molecular Biology 242 (4): 430–55. September 1994. doi:10.1006/jmbi.1994.1593. PMID 7932702.
- ↑ "Structural and phylogenetic analysis of adenovirus hexons by use of high-resolution x-ray crystallographic, molecular modeling, and sequence-based methods". Journal of Virology 77 (17): 9553–66. September 2003. doi:10.1128/jvi.77.17.9553-9566.2003. PMID 12915569.
- ↑ "Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit" (in English). Cell Host & Microbe 6 (6): 523–35. December 2009. doi:10.1016/j.chom.2009.11.006. PMID 20006841.
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