Relation between the flexibility of the WPD loop and the activity of the catalytic domain of protein tyrosine phosphatase SHP-1.
Yang, J
Relation between the flexibility of the WPD loop and the activity of the catalytic domain of protein tyrosine phosphatase SHP-1. [electronic resource] - Journal of cellular biochemistry 2001 - 47-55 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0730-2312
10.1002/jcb.1265 doi
Alanine
Catalytic Domain--physiology
Conserved Sequence--genetics
Enzyme Activation
Intracellular Signaling Peptides and Proteins
Kinetics
Models, Molecular
Mutation
Pliability
Proline
Protein Conformation
Protein Structure, Secondary
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Protein Tyrosine Phosphatases--chemistry
Sequence Homology, Amino Acid
Structure-Activity Relationship
Relation between the flexibility of the WPD loop and the activity of the catalytic domain of protein tyrosine phosphatase SHP-1. [electronic resource] - Journal of cellular biochemistry 2001 - 47-55 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.
0730-2312
10.1002/jcb.1265 doi
Alanine
Catalytic Domain--physiology
Conserved Sequence--genetics
Enzyme Activation
Intracellular Signaling Peptides and Proteins
Kinetics
Models, Molecular
Mutation
Pliability
Proline
Protein Conformation
Protein Structure, Secondary
Protein Tyrosine Phosphatase, Non-Receptor Type 11
Protein Tyrosine Phosphatase, Non-Receptor Type 6
Protein Tyrosine Phosphatases--chemistry
Sequence Homology, Amino Acid
Structure-Activity Relationship