Ontology highlight
ABSTRACT:
SUBMITTER: Heaslet H
PROVIDER: S-EPMC1781954 | biostudies-literature | 2007 Jan
REPOSITORIES: biostudies-literature
Heaslet Holly H Lin Ying-Chuan YC Tam Karen K Torbett Bruce E BE Elder John H JH Stout C David CD
Retrovirology 20070109
We have obtained the 1.7 A crystal structure of FIV protease (PR) in which 12 critical residues around the active site have been substituted with the structurally equivalent residues of HIV PR (12X FIV PR). The chimeric PR was crystallized in complex with the broad-based inhibitor TL-3, which inhibits wild type FIV and HIV PRs, as well as 12X FIV PR and several drug-resistant HIV mutants 1234. Biochemical analyses have demonstrated that TL-3 inhibits these PRs in the order HIV PR > 12X FIV PR > ...[more]