Role of invariant Thr80 in human immunodeficiency virus type 1 protease structure, function, and viral infectivity.

ABSTRACT: Sequence variability associated with human immunodeficiency virus type 1 (HIV-1) is useful for inferring structural and/or functional constraints at specific residues within the viral protease. Positions that are invariant even in the presence of drug selection define critically important residues for protease function. While the importance of conserved active-site residues is easily understood, the role of other invariant residues is not. This work focuses on invariant Thr80 at the apex of the P1 loop of HIV-1, HIV-2, and simian immunodeficiency virus protease. In a previous study, we postulated, on the basis of a molecular dynamics simulation of the unliganded protease, that Thr80 may play a role in the mobility of the flaps of protease. In the present study, both experimental and comput

SUBMITTER: Foulkes JE 

PROVIDER: S-EPMC1489026 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature