Virus coat protein

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<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'>
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'''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.
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'''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. 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]]).

Revision as of 07:29, 27 March 2020

Structure of HIV-I coat protein hexamer (PDB entry 3gv2)

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References

  1. ↑ 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
  2. ↑ 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

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