Binding diversity of a noncovalent-type low-molecular-weight serine protease inhibitor and function of a catalytic water molecule: X-ray crystal structure of PKSI-527-inhibited trypsin

Journal of Biochemistry

Volumn 129, Issue 3, 2001, Pages 455-460

  Tomoo, Koji ^a   Satoh, Kazuhiro ^a   Tsuda, Yuko ^b   Wanaka, Keiko ^c   Okamoto, Shosuke ^c   Hijikata Okunomiya, Akiko ^d   Okada, Yoshio ^b   Ishida, Toshimasa ^a  

^a OSAKA MEDICAL COLLEGE   (Japan)

^b KOBE GAKUIN UNIVERSITY   (Japan)

^c Kobe Research Projects on Thrombosis and Haemostasis   (Japan)

^d KOBE UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Binding diversity; Crystal structure; Noncovalent inhibitor; Trypsin

Indexed keywords

4 AMINOMETHYLCYCLOHEXANECARBONYLPHENYLALANYL 4 AMINOPHENYLACETIC ACID; PHENYLACETIC ACID DERIVATIVE; PKSI 527; SERINE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; TRYPSIN; UNCLASSIFIED DRUG; WATER;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; MOLECULAR WEIGHT; PROTEIN CONFORMATION;

EID: 0035049045     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a002877     Document Type: Article

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