1gwz

<StructureSection load='1gwz' size='340' side='right' caption='[[1gwz]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[1gwz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GWZ FirstGlance]. <br>

</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gwz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwz OCA], [http://pdbe.org/1gwz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gwz RCSB], [http://www.ebi.ac.uk/pdbsum/1gwz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gwz ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/PTN6_HUMAN PTN6_HUMAN]] Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis.<ref>PMID:11266449</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gw/1gwz_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:9774441</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1gwz" style="background-color:#fffaf0;"></div>

*[[Tyrosine phosphatase|Tyrosine phosphatase]]

[[Category: Protein-tyrosine-phosphatase]]

[[Category: Liang, X]]

[[Category: Meng, W]]

[[Category: Niu, T]]

[[Category: Yang, J]]

[[Category: Zhao, Z]]

[[Category: Zhou, G W]]

[[Category: Wpd loop]]