pH-dependent binding modes observed in trypsin crystals: lessons for structure-based drug design.
Stubbs
Milton T
MT
Institut für Pharmazeutische Chemie der Philipps-Universität Marburg, Marbacher Weg 6, 35032 Marburg, Germany. stubbs@mailer.uni-marburg.de
Reyda
Sabine
S
Dullweber
Frank
F
Möller
Maren
M
Klebe
Gerhard
G
Dorsch
Dieter
D
Mederski
Werner W K R
WW
Wurziger
Hanns
H
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D003460:Crystallization; D018360:Crystallography, X-Ray; D015195:Drug Design; D004791:Enzyme Inhibitors / Q000737:chemistry / Q000494:pharmacology*; D015951:Factor Xa / Q000737:chemistry; D065427:Factor Xa Inhibitors; D006863:Hydrogen-Ion Concentration; D008958:Models, Molecular; D013329:Structure-Activity Relationship; D014357:Trypsin / Q000737:chemistry / Q000378:metabolism*
D004791:Enzyme Inhibitors; D065427:Factor Xa Inhibitors; D014357:Trypsin; D015951:Factor Xa