Subsite preferences of retroviral proteinases.
Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville 32610.
B M
BM
Dunn
A
A
Gustchina
A
A
Wlodawer
J
J
Kay
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D002384:Catalysis; D002851:Chromatography, High Pressure Liquid; D015683:Gene Products, gag / Q000378:metabolism; D015684:Gene Products, pol / Q000378:metabolism; D016333:HIV Protease / Q000378:metabolism; D015498:HIV-2 / Q000201:enzymology; D006868:Hydrolysis; D007700:Kinetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism; D010446:Peptide Fragments / Q000032:analysis; D011487:Protein Conformation; D011498:Protein Precursors / Q000378:metabolism; D012190:Retroviridae / Q000201:enzymology* / Q000235:genetics; D016415:Sequence Alignment; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity
D015683:Gene Products, gag; D015684:Gene Products, pol; D009842:Oligopeptides; D010446:Peptide Fragments; D011498:Protein Precursors; D016282:Aspartic Acid Endopeptidases; D016333:HIV Protease; C036946:protease p15