1FIV

STRUCTURE OF AN INHIBITOR COMPLEX OF PROTEINASE FROM FELINE IMMUNODEFICIENCY VIRUS

Summary for 1FIV

• Entry DOI: 10.2210/pdb1fiv/pdb
• Related PRD ID: PRD_000427
• Descriptor: FIV PROTEASE, FIV PROTEASE INHIBITOR ACE-ALN-VAL-STA-GLU-ALN-NH2 (3 entities in total)
• Functional Keywords: acid proteinase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Feline immunodeficiency virus
• Total number of polymer chains: 2
• Total formula weight: 13664.81

Authors

Wlodawer, A.,Gustchina, A.,Reshetnikova, L.,Lubkowski, J.,Zdanov, A. (deposition date: 1995-05-04, release date: 1995-07-31, Last modification date: 2025-03-26)

Primary citation

Wlodawer, A.,Gustchina, A.,Reshetnikova, L.,Lubkowski, J.,Zdanov, A.,Hui, K.Y.,Angleton, E.L.,Farmerie, W.G.,Goodenow, M.M.,Bhatt, D.
Structure of an inhibitor complex of the proteinase from feline immunodeficiency virus.
Nat.Struct.Biol., 2:480-488, 1995

PubMed Abstract: The crystal structure of a recombinant form of the proteinase encoded by the feline immunodeficiency virus (FIV PR) has been solved at 2 A resolution and refined to an R-factor of 0.148. The refined structure includes a peptidomimetic, statine-based inhibitor, LP-149, which is an even more potent inhibitor of HIV PR. Kinetic parameters were obtained for the cleavage of five substrates by FIV PR, and inhibition constants were measured for four inhibitors. The structure of FIV PR resembles other related retroviral enzymes although few inhibitors of HIV PR are capable of inhibiting FIV PR. The structure of FIV PR will enhance our knowledge of this class of enzymes, and will direct testing of new proteinase inhibitors in a feline animal model.

PubMed: 7664111
DOI: 10.1038/nsb0695-480

Experimental method

X-RAY DIFFRACTION (2 Å)