1bvh
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(New page: 200px<br /><applet load="1bvh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bvh" /> '''SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT...)
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Revision as of 09:49, 20 November 2007
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SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE
Overview
Protein tyrosine phosphatases (PTPs) are important enzymes involved in, signal transduction, cell cycle regulation, and the control of, differentiation. Despite the importance of this class of enzymes in the, control of critical cell processes, very little structural information is, available for this family of proteins. In this paper, we present the first, solution structure of a protein tyrosine phosphatase. This protein is a, low molecular weight cytosolic PTP that was initially isolated from bovine, heart. The structure that was determined from 1747 NMR-derived restraints, consists of a central four-stranded parallel beta-sheet surrounded by four, alpha-helices and a short 3(10) helix. The phosphate binding site, identified by chemical shift changes upon the addition of the competitive, inhibitors phosphate and vanadate, is in a loop region connecting the, C-terminal end of the first beta-strand with the first alpha-helix., Residues in the second, fourth, and fifth alpha-helices and in some of the, loop regions connecting the elements of regular secondary structure also, contribute to the binding site. The structure determined here is, consistent with previous mutagenesis and chemical modification studies, conducted on this protein.
About this Structure
1BVH is a Single protein structure of sequence from Bos taurus. Active as Acid phosphatase, with EC number 3.1.3.2 Full crystallographic information is available from OCA.
Reference
Solution structure of a low molecular weight protein tyrosine phosphatase., Logan TM, Zhou MM, Nettesheim DG, Meadows RP, Van Etten RL, Fesik SW, Biochemistry. 1994 Sep 20;33(37):11087-96. PMID:7727361
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