Virus coat protein: Difference between revisions
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The biological assembly of HIV-I coat protein is <scene name='51/516486/Cv/4'>homohexamer</scene> (PDB entry [[3gv2]]). | The biological assembly of HIV-I coat protein is <scene name='51/516486/Cv/4'>homohexamer</scene> (PDB entry [[3gv2]]). | ||
*Adeno-associated virus 9 Vp1 see [[Adeno-Associated Virus]]. | |||
*Ebola virus [[Journal:Acta Cryst F:S2053230X19004424|Structure of the Ebola virus nucleoprotein - RNA complex]] | |||
*Encephalitis virus, Eastern equine see [[FirstGlance/Virus Capsids and Other Large Assemblies#Eastern Equine Encephalitis Virus]] | |||
*[[Hiv-1 gag]] | |||
**[[Tumor susceptibility gene 101]] | |||
*[[Canine parvovirus|Parvovirus, canine]] | |||
*Poliovirus [[Journal:PLoS ONE:1|Antiviral Activity of 3(2H)- and 6-Chloro-3(2H)-Isoflavenes against Highly Diverged, Neurovirulent Vaccine-Derived, Type2 Poliovirus Sewage Isolates]] | |||
*Poliovirus capsid (interactive) at [[FirstGlance/Virus Capsids and Other Large Assemblies]] | |||
*[[Poliovirus receptor-related protein]] | |||
*[[Human rhinovirus|Rhinovirus, human]] | |||
*[[SV40 Capsid Simplified]] | |||
*[[Tobacco Mosaic Virus]] | |||
*[[User:Eric Martz/Virus capsid visualization resources|Virus capsid visualization resources]] | |||
*[[Hugo Heringer de Almeida/5YGH|Zika virus capsid protein]] | |||
==3D structures of virus coat proteins== | ==3D structures of virus coat proteins== | ||
[[Virus coat proteins 3D structures]] | [[Virus coat proteins 3D structures]] | ||
Latest revision as of 17:30, 19 September 2022
Virus coat proteins (VCP) or capsid proteins coat the virus[1]. The various VCPs are designated as Vp1, Vp2, etc. The VCP P domain (protruding domain) in noroviruses binds histo blood group antigen receptors. The outer capsid protein VP4 is a virus spike-forming protein which mediates the virial attachment to the host epithelial cell receptors. The distal portion of Vp4 - Vp8* - is implicated in binding the cellular receptor[2]. VP4 is an outer capsid protein of non-enveloped viruses. VP4 attaches to sialic acid or to integrin heterodimers[3]. VP4 domains include: VP5* which forms the foot of the spike and acts in the permeabilization of the cell membrane and VP8* which forms the head of the spike and binds to sialic acid. The biological assembly of HIV-I coat protein is (PDB entry 3gv2).
3D structures of virus coat proteins |
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ReferencesReferences
- ↑ CASPAR DL, KLUG A. Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol. 1962;27:1-24. doi:, 10.1101/sqb.1962.027.001.005. PMID:14019094 doi:http://dx.doi.org/10.1101/sqb.1962.027.001.005
- ↑ Liu Y, Huang P, Tan M, Liu Y, Biesiada J, Meller J, Castello AA, Jiang B, Jiang X. Rotavirus VP8*: phylogeny, host range, and interaction with histo-blood group antigens. J Virol. 2012 Sep;86(18):9899-910. doi: 10.1128/JVI.00979-12. Epub 2012 Jul 3. PMID:22761376 doi:http://dx.doi.org/10.1128/JVI.00979-12
- ↑ Mackow ER, Barnett JW, Chan H, Greenberg HB. The rhesus rotavirus outer capsid protein VP4 functions as a hemagglutinin and is antigenically conserved when expressed by a baculovirus recombinant. J Virol. 1989 Apr;63(4):1661-8. PMID:2538649