X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity

Journal of Biological Chemistry

Volumn 274, Issue 53, 1999, Pages 37862-37868

  Dajani, Rana ^a,d   Cleasby, Anne ^b   Margarete, Neu ^b   Wonacott, Alan J ^b   Jhoti, Harren ^b   Hood, Alan M ^a   Modi, Sandeep ^b   Hersey, Anne ^b   Taskinen, Jyrki ^c   Cooke, Robert M ^b   Manchee, Gary R ^b   Coughtrie, Michael W H ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

^b GLAXOSMITHKLINE   (United Kingdom)

^c UNIVERSITY OF HELSINKI   (Finland)

^d INSTITUTE OF CANCER RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

DOPAMINE SULFOTRANSFERASE; ESTROGEN SULFOTRANSFERASE; SULFOTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HUMAN; HUMAN CELL; HYDROGEN BOND; MOLECULAR MODEL; PRIORITY JOURNAL; PROTEIN INTERACTION; QUANTITATIVE STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

ALANINE; AMINO ACID SUBSTITUTION; ARYLSULFOTRANSFERASE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; GLUTAMIC ACID; HUMANS; KINETICS; MODELS, MOLECULAR; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

EID: 0033621476     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.53.37862     Document Type: Article

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