Time dependent heterodimer formation leads to inhibition of HIV protease activity.
Babé
L M
LM
Department of Pharmaceutical Chemistry, University of California, San Francisco 94143-0446.
Craik
C S
CS
D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry / Q000235:genetics; D016333:HIV Protease / Q000737:chemistry / Q000235:genetics; D017320:HIV Protease Inhibitors; D015497:HIV-1 / Q000201:enzymology / Q000235:genetics; D015498:HIV-2 / Q000201:enzymology / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
D017320:HIV Protease Inhibitors; D011994:Recombinant Proteins; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C065184:p16 protease, Human immunodeficiency virus 2