Summary for 1A8O
Entry DOI | 10.2210/pdb1a8o/pdb |
Descriptor | HIV CAPSID (2 entities in total) |
Functional Keywords | capsid, core protein, hiv, c-terminal domain, viral protein |
Biological source | Human immunodeficiency virus 1 |
Cellular location | Gag-Pol polyprotein: Host cell membrane; Lipid-anchor . Matrix protein p17: Virion membrane; Lipid- anchor . Capsid protein p24: Virion . Nucleocapsid protein p7: Virion . Reverse transcriptase/ribonuclease H: Virion . Integrase: Virion : P12497 |
Total number of polymer chains | 1 |
Total formula weight | 8175.72 |
Authors | Gamble, T.R.,Yoo, S.,Vajdos, F.F.,Von Schwedler, U.K.,Worthylake, D.K.,Wang, H.,Mccutcheon, J.P.,Sundquist, W.I.,Hill, C.P. (deposition date: 1998-03-27, release date: 1998-10-14, Last modification date: 2024-10-30) |
Primary citation | Gamble, T.R.,Yoo, S.,Vajdos, F.F.,von Schwedler, U.K.,Worthylake, D.K.,Wang, H.,McCutcheon, J.P.,Sundquist, W.I.,Hill, C.P. Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science, 278:849-853, 1997 Cited by PubMed Abstract: The carboxyl-terminal domain, residues 146 to 231, of the human immunodeficiency virus-1 (HIV-1) capsid protein [CA(146-231)] is required for capsid dimerization and viral assembly. This domain contains a stretch of 20 residues, called the major homology region (MHR), which is conserved across retroviruses and is essential for viral assembly, maturation, and infectivity. The crystal structures of CA(146-231) and CA(151-231) reveal that the globular domain is composed of four helices and an extended amino-terminal strand. CA(146-231) dimerizes through parallel packing of helix 2 across a dyad. The MHR is distinct from the dimer interface and instead forms an intricate hydrogen-bonding network that interconnects strand 1 and helices 1 and 2. Alignment of the CA(146-231) dimer with the crystal structure of the capsid amino-terminal domain provides a model for the intact protein and extends models for assembly of the central conical core of HIV-1. PubMed: 9346481DOI: 10.1126/science.278.5339.849 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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