3DIK
Pseudo-atomic model of the HIV-1 CA hexameric lattice
Summary for 3DIK
| Entry DOI | 10.2210/pdb3dik/pdb |
| EMDB information | 1529 |
| Descriptor | Capsid protein p24 (1 entity in total) |
| Functional Keywords | 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, viral protein |
| Biological source | Human immunodeficiency virus type 1 |
| Total number of polymer chains | 1 |
| Total formula weight | 24498.08 |
| Authors | Ganser-Pornillos, B.K.,Cheng, A.,Yeager, M. (deposition date: 2008-06-20, release date: 2008-09-16, Last modification date: 2024-02-21) |
| Primary citation | Ganser-Pornillos, B.K.,Cheng, A.,Yeager, M. Structure of full-length HIV-1 CA: a model for the mature capsid lattice Cell(Cambridge,Mass.), 131:70-79, 2007 Cited by PubMed Abstract: 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. PubMed: 17923088DOI: 10.1016/j.cell.2007.08.018 PDB entries with the same primary citation |
| Experimental method | ELECTRON CRYSTALLOGRAPHY (9 Å) |
Structure validation
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