2hnp
From Proteopedia
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| - | [[Image:2hnp.jpg|left|200px]] | + | [[Image:2hnp.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B''' | + | {{Structure |
| + | |PDB= 2hnp |SIZE=350|CAPTION= <scene name='initialview01'>2hnp</scene>, resolution 2.85Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |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= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HNP is a [ | + | 2HNP 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=2HNP OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of human protein tyrosine phosphatase 1B., Barford D, Flint AJ, Tonks NK, Science. 1994 Mar 11;263(5152):1397-404. PMID:[http:// | + | Crystal structure of human protein tyrosine phosphatase 1B., Barford D, Flint AJ, Tonks NK, Science. 1994 Mar 11;263(5152):1397-404. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8128219 8128219] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
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[[Category: hydrolase(phosphorylation)]] | [[Category: hydrolase(phosphorylation)]] | ||
| - | ''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 17:19:12 2008'' |
Revision as of 15:19, 20 March 2008
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| , resolution 2.85Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B
Contents |
Overview
Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation.
Disease
Known diseases associated with this structure: Abdominal body fat distribution, modifier of OMIM:[176885], Insulin resistance, susceptibility to OMIM:[176885]
About this Structure
2HNP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of human protein tyrosine phosphatase 1B., Barford D, Flint AJ, Tonks NK, Science. 1994 Mar 11;263(5152):1397-404. PMID:8128219
Page seeded by OCA on Thu Mar 20 17:19:12 2008
