2hnp
From Proteopedia
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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. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 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 Fri Feb 15 17:32:50 2008
