Structure-function database for active site binding to the aspartic proteinases.
Rao
C
C
Department of Biochemistry & Molecular Biology, University of Florida, Gainesville 32610.
Scarborough
P E
PE
Lowther
W T
WT
Kay
J
J
Batley
B
B
Rapundalo
S
S
Klutchko
S
S
Taylor
M D
MD
Dunn
B M
BM
D000595:Amino Acid Sequence; D000818:Animals; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D020059:Cathepsin E; D002403:Cathepsins / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D016208:Databases, Factual; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000494:pharmacology; D010434:Pepsin A / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
D009842:Oligopeptides; D002403:Cathepsins; D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A; D020059:Cathepsin E