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1phr
From Proteopedia
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'''THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE''' | '''THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE''' | ||
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[[Category: Su, X D.]] | [[Category: Su, X D.]] | ||
[[Category: Taddei, N.]] | [[Category: Taddei, N.]] | ||
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:06:01 2008'' | |
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Revision as of 02:06, 3 May 2008
THE CRYSTAL STRUCTURE OF A LOW MOLECULAR PHOSPHOTYROSINE PROTEIN PHOSPHATASE
Overview
Protein tyrosine phosphorylation and dephosphorylation are central reactions for control of cellular division, differentiation and development. Here we describe the crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase (PTPase), a cytosolic phosphatase present in many mammalian cells. The enzyme catalyses the dephosphorylation of phosphotyrosine-containing substrates, and overexpression of the protein in normal and transformed cells inhibits cell proliferation. The structure of the low-molecular-weight PTPase reveals an alpha/beta protein containing a phosphate-binding loop motif at the amino end of helix alpha 1. This motif includes the essential active-site residues Cys 12 and Arg 18 and bears striking similarities to the active-site motif recently described in the structure of human PTP1B. The structure of the low-molecular-weight PTPase supports a reaction mechanism involving the conserved Cys 12 as an attacking nucleophile in an in-line associative mechanism. The structure also suggests a catalytic role for Asp 129 in the reaction cycle.
About this Structure
1PHR is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase., Su XD, Taddei N, Stefani M, Ramponi G, Nordlund P, Nature. 1994 Aug 18;370(6490):575-8. PMID:8052313 Page seeded by OCA on Sat May 3 05:06:01 2008
