Enzyme flexibility, solvent and 'weak' interactions characterize thrombin-ligand interactions: Implications for drug design

Structure

Volumn 4, Issue 11, 1996, Pages 1353-1362

  Engh, Richard A ^a   Brandstetter, Hans ^a,c   Sucher, Gudrun ^a   Eichinger, Andreas ^a   Baumann, Ulrich ^a,d   Bode, Wolfram ^a   Huber, Robert ^a   Poll, Thomas ^b   Rudolph, Rainer ^b,e   Von Der Saal, Wolfgang ^b  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

^b F HOFFMANN LA ROCHE LTD   (Switzerland)

^c MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

^d INSTITUTE OF CANCER RESEARCH   (United Kingdom)

^e MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

anticoagulant; drug design; protein flexibility; thrombin; weak interactions; X ray crystallography

Indexed keywords

ANIMALIA; BOS TAURUS;

EID: 16144365754     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(96)00142-6     Document Type: Article

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