Virus coat protein: Difference between revisions

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**[[2i2s]] - VCP Vp4 Vp8* domain – pig rotavirus<br />
**[[2i2s]] - VCP Vp4 Vp8* domain – pig rotavirus<br />
**[[3sis]], [[3sit]] - prVCP Vp4 Vp8* domain + glycan<br />
**[[3sis]], [[3sit]] - prVCP Vp4 Vp8* domain + glycan<br />
**[[2dwr]] - hrvVCP Vp8* – human rotavirus<br />
**[[2dwr]] - hrvVCP Vp4 Vp8* domain – human rotavirus<br />
**[[4drr]], [[4drv]], [[4ds0]] - hrvVCP Vp4 Vp8* domain + antigen
**[[4drr]], [[4drv]], [[4ds0]] - hrvVCP Vp4 Vp8* domain + antigen



Revision as of 11:22, 14 December 2016


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. VP4 is an outer capsid protein of non-enveloped viruses. VP4 attaches to sialic acid or to integrin heterodimers[2]. 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.

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

Drag the structure with the mouse to rotate

3D structures of virus coat proteins3D structures of virus coat proteins

Updated on 14-December-2016

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

Michal Harel, Alexander Berchansky, Joel L. Sussman