1gwz
From Proteopedia
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CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF THE PROTEIN TYROSINE PHOSPHATASE SHP-1
Overview
The crystal structures of the protein-tyrosine phosphatase SHP-1 catalytic, domain and the complex it forms with the substrate analogue tungstate have, been determined and refined to crystallographic R values of 0.209 at 2.5 A, resolution and 0.207 at 2.8 A resolution, respectively. Despite low, sequence similarity, the catalytic domain of SHP-1 shows high similarity, in secondary and tertiary structures with other protein-tyrosine, phosphatases (PTPs). In contrast to the conformational changes observed in, the crystal structures of PTP1B and Yersinia PTP, the WPD loop, (Trp419-Pro428) in the catalytic domain of SHP-1 moves away from the, substrate binding pocket after binding the tungstate ion. Sequence, alignment and structural analysis suggest that the residues in the WPD, loop, especially the amino acid following Asp421, are critical for the, movement of WPD loop on binding substrates and the specific activity of, protein-tyrosine phosphatases. Our mutagenesis and kinetic measurements, have supported this hypothesis.
About this Structure
1GWZ is a Single protein structure of sequence from Homo sapiens. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1., Yang J, Liang X, Niu T, Meng W, Zhao Z, Zhou GW, J Biol Chem. 1998 Oct 23;273(43):28199-207. PMID:9774441
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