2hnp

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[[Image:2hnp.jpg|left|200px]]
[[Image:2hnp.jpg|left|200px]]
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{{Structure
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|PDB= 2hnp |SIZE=350|CAPTION= <scene name='initialview01'>2hnp</scene>, resolution 2.85&Aring;
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The line below this paragraph, containing "STRUCTURE_2hnp", creates the "Structure Box" on the page.
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <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>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hnp OCA], [http://www.ebi.ac.uk/pdbsum/2hnp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hnp RCSB]</span>
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'''CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B'''
'''CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B'''
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[[Category: Flint, A J.]]
[[Category: Flint, A J.]]
[[Category: Tonks, N K.]]
[[Category: Tonks, N K.]]
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[[Category: hydrolase(phosphorylation)]]
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Revision as of 03:29, 4 May 2008

Template:STRUCTURE 2hnp

CRYSTAL STRUCTURE OF HUMAN PROTEIN TYROSINE PHOSPHATASE 1B


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.

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 Sun May 4 06:29:38 2008

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