Identification of Structural Motifs and Amino Acids within the Structure of Human Heparan Sulfate 3-O-Sulfotransferase That Mediate Enzymatic Function
Copyright policy )Identification of Structural Motifs and Amino Acids within the Structure of Human Heparan Sulfate 3-O-Sulfotransferase That Mediate Enzymatic Function
In an accompanying paper [J. R. Myette, Z. Shriver, J. Liu, G. Venkataraman, and R. Sasisekharan (2002) Biochem. Biophys. Res. Commun. 290, 1206-1213], we described the purification and biochemical characterization of a soluble, recombinantly expressed form of the human heparan sulfate 3-O-sulfotransferase (3-OST-1). Such an important first step enables detailed structure-function studies for this class of enzymes. Herein, we describe a complimentary, structure-based homology modeling approach for predicting 3-OST-1 structure. This approach employs a variety of structural analysis and molecular modeling tools used in conjunction with protein crystallographic studies of related enzymes. In this manner, we describe important motifs within the predicted three-dimensional structure of the enzyme and identify specific amino acids that are likely important for enzymatic function.
- Massachusetts Institute of Technology United States
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Protein Conformation, Amino Acid Motifs, Molecular Sequence Data, In Vitro Techniques, Recombinant Proteins, Adenosine Diphosphate, Catalytic Domain, Cystine, Humans, Amino Acid Sequence, Sulfotransferases, Nucleoside-Phosphate Kinase
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Protein Conformation, Amino Acid Motifs, Molecular Sequence Data, In Vitro Techniques, Recombinant Proteins, Adenosine Diphosphate, Catalytic Domain, Cystine, Humans, Amino Acid Sequence, Sulfotransferases, Nucleoside-Phosphate Kinase
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