Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein

Theresa R. Gamble, Sanghee Yoo, Felix F. Vajdos, Uta K. Von Schwedler, David K. Worthylake, Hui Wang, John P. McCutcheon, Wesley I. Sundquist, Christopher P. Hill

Research output: Contribution to journalArticlepeer-review

516 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)849-853
Number of pages5
Issue number5339
StatePublished - Oct 31 1997
Externally publishedYes

ASJC Scopus subject areas

  • General


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