Virus coat protein: Difference between revisions

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Michal Harel, Alexander Berchansky, Joel L. Sussman

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	<StructureSection load='~~3gv2~~' 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: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.