1bvh: Difference between revisions

Revision as of 19:46, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1bvh.png

Template:STRUCTURE 1bvh

SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASESOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE

Template:ABSTRACT PUBMED 7727361

About this StructureAbout this Structure

1BVH is a Single protein structure of sequence from Bos taurus. Full experimental information is available from OCA.

ReferenceReference

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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-'''SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE'''
+===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.
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+(as it appears on PubMed at http://www.pubmed.gov), where 7727361 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_7727361}}
 ==About this Structure==
-BVH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVH OCA].
+BVH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BVH OCA].
 ==Reference==
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 [[Category: Zhou, M M.]]
 [[Category: Hydrolase]]
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