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Virus coat protein
From Proteopedia
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| - | <StructureSection load='3gv2' size='350' side='right' caption='Structure of HIV-I coat protein hexamer (PDB entry [[3gv2]])' scene=''> | + | <StructureSection load='3gv2' 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: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. | ||
Revision as of 09:35, 27 July 2017
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3D structures of virus coat proteins
Updated on 27-July-2017
