The structure of truncated recombinant human bile salt-stimulated lipase reveals bile salt-independent conformational flexibility at the active-site loop and provides insights into heparin binding

Journal of Molecular Biology

Volumn 312, Issue 3, 2001, Pages 511-523

  Moore, Stanley A ^a   Kingston, Richard L ^a   Loomes, Kerry M ^b   Hernell, Olle ^c   Bläckberg, Lars ^c   Baker, Heather M ^a   Baker, Edward N ^a  

^a MASSEY UNIVERSITY   (New Zealand)

^b UNIVERSITY OF AUCKLAND   (New Zealand)

^c UMEÅ UNIVERSITY   (Sweden)

Author keywords

Bile salt dependent lipase; Bile salt stimulated lipase; Carboxyl ester lipase; Cholesterol esterase; Heparin

Indexed keywords

3 [(3 CHOLAMIDOPROPYL)DIMETHYLAMMONIO] 1 PROPANESULFONIC ACID; BILE ACID; BILE SALT; BILE SALT STIMULATED LIPASE; DEOXYCHOLIC ACID; HEPARIN; SULFONIC ACID DERIVATIVE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME STRUCTURE; HUMAN; PRIORITY JOURNAL; PROTEIN BINDING;

EID: 0035929324     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4979     Document Type: Article

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