2shp: Difference between revisions
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[[Image:2shp.gif|left|200px]] | [[Image:2shp.gif|left|200px]] | ||
'''TYROSINE PHOSPHATASE SHP-2''' | {{Structure | ||
|PDB= 2shp |SIZE=350|CAPTION= <scene name='initialview01'>2shp</scene>, resolution 2.00Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CAT:DODECANE-TRIMETHYLAMINE'>CAT</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''TYROSINE PHOSPHATASE SHP-2''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2SHP is a [ | 2SHP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SHP OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9491886 9491886] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
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[[Category: tyrosine phosphatase]] | [[Category: tyrosine phosphatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:38:25 2008'' | ||
Revision as of 16:38, 20 March 2008
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| 2shp, resolution 2.00Å | |||||||||||||
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| Ligands: | CAT | ||||||||||||
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
TYROSINE PHOSPHATASE SHP-2
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. 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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