PMID:19523676

Citation	Pornillos, O, Ganser-Pornillos, BK, Kelly, BN, Hua, Y, Whitby, FG, Stout, CD, Sundquist, WI, Hill, CP and Yeager, M (2009) X-ray structures of the hexameric building block of the HIV capsid. Cell 137:1282-92
Abstract	The mature capsids of HIV and other retroviruses organize and package the viral genome and its associated enzymes for delivery into host cells. The HIV capsid is a fullerene cone: a variably curved, closed shell composed of approximately 250 hexamers and exactly 12 pentamers of the viral CA protein. We devised methods for isolating soluble, assembly-competent CA hexamers and derived four crystallographically independent models that define the structure of this capsid assembly unit at atomic resolution. A ring of six CA N-terminal domains form an apparently rigid core, surrounded by an outer ring of C-terminal domains. Mobility of the outer ring appears to be an underlying mechanism for generating the variably curved lattice in authentic capsids. Hexamer-stabilizing interfaces are highly hydrated, and this property may be key to the formation of quasi-equivalent interactions within hexamers and pentamers. The structures also clarify the molecular basis for capsid assembly inhibition and should facilitate structure-based drug design strategies.
Links	PubMed PMC2840706 Online version:10.1016/j.cell.2009.04.063
Keywords	Capsid Proteins/chemistry; Capsid Proteins/metabolism; Crystallography, X-Ray; HIV-1/chemistry; HIV-1/metabolism; Models, Molecular; Polymers/metabolism; Protein Structure, Tertiary
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
HV1N5:POL	enables	GO:0042802: identical protein binding	ECO:0000353: physical interaction evidence used in manual assertion	UniProtKB:P12497:PRO_0000042395	F		Seeded From UniProt	complete

References

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