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From Proteopedia
HIV-1 CRF07 gp41
Structural highlights
Function[Q994K2_9HIV1] The envelope glyprotein gp160 precursor down-modulates cell surface CD4 antigen by interacting with it in the endoplasmic reticulum and blocking its transport to the cell surface (By similarity).[RuleBase:RU004292][SAAS:SAAS000328_004_020447] The gp120-gp41 heterodimer allows rapid transcytosis of the virus through CD4 negative cells such as simple epithelial monolayers of the intestinal, rectal and endocervical epithelial barriers. Both gp120 and gp41 specifically recognize glycosphingolipids galactosyl-ceramide (GalCer) or 3' sulfo-galactosyl-ceramide (GalS) present in the lipid rafts structures of epithelial cells. Binding to these alternative receptors allows the rapid transcytosis of the virus through the epithelial cells. This transcytotic vesicle-mediated transport of virions from the apical side to the basolateral side of the epithelial cells does not involve infection of the cells themselves (By similarity). Publication Abstract from PubMedHIV CRF07 B'/C is a strain circulating mainly in northwest region of China. The gp41 region of CRF07 is derived from a clade C virus. In order to compare the difference of CRF07 gp41 with that of typical clade B virus, we solved the crystal structure of the core region of CRF07 gp41. Compared with clade B gp41, CRF07 gp41 evolved more basic and hydrophilic residues on its helix bundle surface. Based on sequence alignment, a hyper-mutant cluster located in the middle of HR2 heptads repeat was identified. The mutational study of these residues revealed that this site is important in HIV mediated cell-cell fusion and plays critical roles in conformational changes during viral invasion. The crystal structure of HIV CRF07 B'/C gp41 reveals a hyper-mutant site in the middle of HR2 heptad repeat.,Du J, Xue H, Ma J, Liu F, Zhou J, Shao Y, Qiao W, Liu X Virology. 2013 Nov;446(1-2):86-94. doi: 10.1016/j.virol.2013.07.024. Epub 2013, Aug 25. PMID:24074570[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Du, J | Liu, F | Liu, X | Ma, J | Qiao, W | Shao, Y | Xue, H | Zhou, J | Alpha-helix | Double helix | Glycoprotein | Membrane | Viral protein | Virus fusion
