View source for 1bvh

==SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE==
<StructureSection load='1bvh' size='340' side='right' caption='[[1bvh]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bvh]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BVH FirstGlance]. <br>
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bvh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bvh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bvh RCSB], [http://www.ebi.ac.uk/pdbsum/1bvh PDBsum]</span></td></tr>
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== Function ==
[[http://www.uniprot.org/uniprot/PPAC_BOVIN PPAC_BOVIN]] Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. 
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bv/1bvh_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:7727361</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
*[[Acid phosphatase|Acid phosphatase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acid phosphatase]]
[[Category: Bos taurus]]
[[Category: Etten, R L.Van]]
[[Category: Fesik, S W]]
[[Category: Logan, T M]]
[[Category: Meadows, R P]]
[[Category: Nettesheim, D G]]
[[Category: Zhou, M M]]
[[Category: Hydrolase]]