2shp
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(New page: 200px<br /> <applet load="2shp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2shp, resolution 2.00Å" /> '''TYROSINE PHOSPHATAS...)
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Revision as of 21:31, 12 November 2007
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TYROSINE PHOSPHATASE SHP-2
Contents |
Overview
The structure of the SHP-2 tyrosine phosphatase, determined at 2.0, angstroms resolution, shows how its catalytic activity is regulated by its, two SH2 domains. In the absence of a tyrosine-phosphorylated binding, partner, the N-terminal SH2 domain binds the phosphatase domain and, directly blocks its active site. This interaction alters the structure of, the N-SH2 domain, disrupting its phosphopeptide-binding cleft. Conversely, interaction of the N-SH2 domain with phosphopeptide disrupts its, phosphatase recognition surface. Thus, the N-SH2 domain is a, conformational switch; it either binds and inhibits the phosphatase, or it, binds phosphoproteins and activates the enzyme. Recognition of, bisphosphorylated ligands by the tandem SH2 domains is an integral element, of this switch; the C-terminal SH2 domain contributes binding energy and, specificity, but it does not have a direct role in activation.
Disease
Known diseases associated with this structure: Leopard syndrome OMIM:[176876], Leukemia, juvenile myelomonocytic OMIM:[176876], Noonan syndrome 1 OMIM:[176876]
About this Structure
2SHP is a Single protein structure of sequence from Homo sapiens with CAT as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 Full crystallographic information is available from OCA.
Reference
Crystal structure of the tyrosine phosphatase SHP-2., Hof P, Pluskey S, Dhe-Paganon S, Eck MJ, Shoelson SE, Cell. 1998 Feb 20;92(4):441-50. PMID:9491886
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