X-ray structures of retroviral proteases and their inhibitor-bound complexes.
Ringe
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Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, Massachusetts 02254.
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D018360:Crystallography, X-Ray; D015195:Drug Design; D016333:HIV Protease / Q000737:chemistry / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000378:metabolism; D015497:HIV-1 / Q000201:enzymology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010436:Pepstatins / Q000737:chemistry; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D012190:Retroviridae / Q000201:enzymology*; D012191:Retroviridae Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism; D013329:Structure-Activity Relationship
D017320:HIV Protease Inhibitors; D010436:Pepstatins; D010455:Peptides; D012191:Retroviridae Proteins; C014195:Streptomyces pepsin inhibitor; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C031375:pepstatin