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TitleStructure of full-length HIV-1 CA: a model for the mature capsid lattice.
Journal, issue, pagesCell, Vol. 131, Issue 1, Page 70-79, Year 2007
Publish dateOct 5, 2007
AuthorsBarbie K Ganser-Pornillos / Anchi Cheng / Mark Yeager /
PubMed AbstractThe capsids of mature retroviruses perform the essential function of organizing the viral genome for efficient replication. These capsids are modeled as fullerene structures composed of closed ...The capsids of mature retroviruses perform the essential function of organizing the viral genome for efficient replication. These capsids are modeled as fullerene structures composed of closed hexameric arrays of the viral CA protein, but a high-resolution structure of the lattice has remained elusive. A three-dimensional map of two-dimensional crystals of the R18L mutant of HIV-1 CA was derived by electron cryocrystallography. The docking of high-resolution domain structures into the map yielded the first unambiguous model for full-length HIV-1 CA. Three important protein-protein assembly interfaces are required for capsid formation. Each CA hexamer is composed of an inner ring of six N-terminal domains and an outer ring of C-terminal domains that form dimeric linkers connecting neighboring hexamers. Interactions between the two domains of CA further stabilize the hexamer and provide a structural explanation for the mechanism of action of known HIV-1 assembly inhibitors.
External linksCell / PubMed:17923088
MethodsEM (electron crystallography)
Resolution9.0 Å
Structure data

1529

3dik

EMDB-1529: Structure of Full-Length HIV-1 CA.
PDB-3dik: Pseudo-atomic model of the HIV-1 CA hexameric lattice
Method: EM (electron crystallography) / Resolution: 9.0 Å

Source
  • Human immunodeficiency virus 1
  • human immunodeficiency virus type 1
KeywordsVIRAL PROTEIN / MATURE RETROVIRAL CAPSID / FULLERENE CONE / HEXAMER / AIDS / Aspartyl protease / Capsid maturation / Capsid protein / DNA integration / DNA recombination / DNA-directed DNA polymerase / Endonuclease / Hydrolase / Lipoprotein / Magnesium / Metal-binding / Multifunctional enzyme / Myristate / Nuclease / Nucleotidyltransferase / Nucleus / Phosphoprotein / Protease / RNA-binding / RNA-directed DNA polymerase / Transferase / Viral nucleoprotein / Virion / Zinc-finger

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