Virus coat protein: Difference between revisions

Michal Harel (talk | contribs)
No edit summary
No edit summary
 
(8 intermediate revisions by 2 users not shown)
Line 1: Line 1:
<StructureSection load='' size='350' side='right' caption='Structure of HIV-I coat protein hexamer (PDB entry [[3gv2]])' scene='51/516486/Cv/1'>
<StructureSection load='' size='350' side='right' caption='Structure of HIV-I coat protein hexamer (PDB entry [[3gv2]])' scene='51/516486/Cv/1'>


'''Virus coat proteins''' (VCP) or capsid proteins coat the virus<ref>PMID:19825049</ref>.  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.  VP4 is an outer capsid protein of non-enveloped viruses. VP4 attaches to sialic acid or to integrin heterodimers<ref>PMID:2538649</ref>.  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.
'''Virus coat proteins''' (VCP) or '''capsid proteins''' coat the virus<ref>PMID:14019094</ref>.  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<ref>PMID:22761376</ref>.  VP4 is an outer capsid protein of non-enveloped viruses. VP4 attaches to sialic acid or to integrin heterodimers<ref>PMID:2538649</ref>.  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 <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]]).


For details on Zika virus capsid protein see [[Hugo Heringer de Almeida/5YGH]].
*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]]


For adeno-associated virus 9 Vp1 see [[Adeno-Associated Virus]].
See also [[Viral capsids]]
==3D structures of virus coat proteins==
==3D structures of virus coat proteins==
[[Virus coat proteins 3D structures]]
[[Virus coat proteins 3D structures]]

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman