Refined 2·3ÅX-ray crystal structure of bovine thrombin complexes formed with the benzamidine and arginine-based thrombin inhibitors NAPAP, 4-TAPAP and MQPA
Authors:
- Hans BrandstetterHBHans Brandstetter
- Dusan TurkDTDusan Turk
- H. Wolfgang HoeffkenHHH. Wolfgang Hoeffken
- Doris GrosseDGDoris Grosse
- Jörg StürzebecherJSJörg Stürzebecher
- Philip D. MartinPMPhilip D. Martin
- Brian F.P. EdwardsBEBrian F.P. Edwards
- Wolfram BodeWBWolfram Bode
- 1 August 1992
- journal article
- research article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 226 (4) , 1085-1099
Abstract
No abstract availableKeywords
Funding Information
- Verband der Chemischen Industrie
This publication has 48 references indexed in Scilit:
- Refined structure of the Hirudin-thrombin complexJournal of Molecular Biology, 1991
- Geometry of binding of the Nα‐tosylated piperidides of m‐amidino‐, p‐amidino‐ and p‐guanidino phenylalanine to thrombin and trypsinFEBS Letters, 1991
- Geometry of binding of the benzamidine‐ and arginine‐based inhibitors Nα‐(2‐naphthyl‐sulphonyl‐glycyl)‐dl‐p‐amidinophenylalanyl‐piperidine (NAPAP) and (2R,4R)‐4‐methyl‐1‐[Nα‐(3‐methyl‐1,2,3,4‐tetrahydro‐8‐quinolinesulphonyl)‐l‐arginyl]‐2‐piperidine carboxylic acid (MQPA) to human α‐thrombinEuropean Journal of Biochemistry, 1990
- Structure and evolution of the bovine prothrombin geneJournal of Molecular Biology, 1988
- Potent inhibition of thrombin by the newly synthesized arginine derivative No. 805. The importance of stereo-structure of its hydrophobic carboxamide portionBiochemical and Biophysical Research Communications, 1981
- Thrombin inhibitors. 1. Ester derivatives of N.alpha.-(arylsulfonyl)-L-arginineJournal of Medicinal Chemistry, 1980
- Conformation of amino acid side-chains in proteinsJournal of Molecular Biology, 1978
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- The refined crystal structure of bovine β-trypsin at 1·8 Å resolutionJournal of Molecular Biology, 1975
- On the size of the active site in proteases. I. PapainBiochemical and Biophysical Research Communications, 1967