Structural and theoretical studies suggest domain movement produces an active conformation of thymidine phosphorylase

Journal of Molecular Biology

Volumn 281, Issue 2, 1998, Pages 285-299

  Pugmire, Matthew J ^a   Cook, William J ^c,d   Jasanoff, Alan ^b   Walter, Mark R ^d   Ealick, Steven E ^b  

^a Department of Molecular Biology and Genetics   (United States)

^b Department of Obstetrics Gynecology   (United States)

^c University of Alabama at Birmingham   (United States)

^d UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

Crystallography; Flexible domain movement; Platelet derived endothelial cell growth factor; Thymidine phosphorylase

Indexed keywords

GLYCINE; HISTIDINE; PHOSPHATE; THYMIDINE PHOSPHORYLASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ESCHERICHIA COLI; HYDROGEN BOND; MODEL; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; THEORETICAL STUDY;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032516763     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1941     Document Type: Article

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