Comparisons of the sequences, 3-D structures and mechanisms of pepsin-like and retroviral aspartic proteinases.
Blundell
T L
TL
Imperial Cancer Research Fund Unit of Structural Molecular Biology, Birkbeck College, University of London, United Kingdom.
Cooper
J B
JB
Sali
A
A
Zhu
Z Y
ZY
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000235:genetics; D001665:Binding Sites; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010434:Pepsin A / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics; D010802:Phylogeny; D011487:Protein Conformation; D012190:Retroviridae / Q000201:enzymology / Q000235:genetics; D016415:Sequence Alignment
D016282:Aspartic Acid Endopeptidases; D010434:Pepsin A