1AUM

HIV CAPSID C-TERMINAL DOMAIN (CAC146)

Summary for 1AUM

• Entry DOI: 10.2210/pdb1aum/pdb
• Descriptor: HIV CAPSID (1 entity in total)
• Functional Keywords: core protein, hiv, capsid, c-terminal domain, cac146, viral protein
• Biological source: Human immunodeficiency virus 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: 7970.10

Authors

Hill, C.P.,Gamble, T.R.,Yoo, S.,Vajdos, F.F.,Von Schwedler, U.K.,Worthylake, D.K.,Wang, H.,Mccutcheon, J.P.,Sundquist, W.I. (deposition date: 1997-08-29, release date: 1998-01-14, Last modification date: 2024-10-09)

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

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: 9346481
DOI: 10.1126/science.278.5339.849

Experimental method

X-RAY DIFFRACTION (3 Å)