Flexibility in HIV-1 assembly subunits: solution structure of the monomeric C-terminal domain of the capsid protein.

ABSTRACT: The protein CA forms the mature capsid of human immunodeficiency virus. Hexamerization of the N-terminal domain and dimerization of the C-terminal domain, CAC, occur during capsid assembly, and both domains constitute potential targets for anti-HIV inhibitors. CAC homodimerization occurs mainly through its second helix, and is abolished when its sole tryptophan is mutated to alanine. Previous thermodynamic data obtained with the dimeric and monomeric forms of CAC indicate that the structure of the mutant resembles that of a monomeric intermediate found in the folding and association reactions of CAC. We have solved the three-dimensional structure in aqueous solution of the monomeric mutant. The structure is similar to that of the subunits in the dimeric, nonmutated CAC, except the segment

SUBMITTER: Alcaraz LA 

PROVIDER: S-EPMC1929042 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature