3H47

X-ray Structure of Hexameric HIV-1 CA

Summary for 3H47

• Entry DOI: 10.2210/pdb3h47/pdb
• Related: 3GV2 3H4E
• Descriptor: Capsid protein p24 (2 entities in total)
• Functional Keywords: capsid protein, hexamer, engineered disulfide bonds, viral protein
• Biological source: Human immunodeficiency virus type 1 (NEW YORK-5 ISOLATE) (HIV-1)
• Cellular location: Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P12497
• Total number of polymer chains: 1
• Total formula weight: 25461.27

Authors

Pornillos, O. (deposition date: 2009-04-18, release date: 2009-06-23, Last modification date: 2023-09-06)

Primary citation

Pornillos, O.,Ganser-Pornillos, B.K.,Kelly, B.N.,Hua, Y.,Whitby, F.G.,Stout, C.D.,Sundquist, W.I.,Hill, C.P.,Yeager, M.
X-ray structures of the hexameric building block of the HIV capsid.
Cell(Cambridge,Mass.), 137:1282-1292, 2009

PubMed 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.

PubMed: 19523676
DOI: 10.1016/j.cell.2009.04.063

Experimental method

X-RAY DIFFRACTION (1.9 Å)