View source for 2gjy


==NMR Solution Structure of Tensin1 PTB Domain==
<StructureSection load='2gjy' size='340' side='right'caption='[[2gjy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2gjy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GJY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2gjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gjy OCA], [https://pdbe.org/2gjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gjy RCSB], [https://www.ebi.ac.uk/pdbsum/2gjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gjy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TENS1_CHICK TENS1_CHICK] May act as a protein phosphatase and/or a lipid phosphatase. Involved in fibrillar adhesion formation. Plays a role in cell polarization and migration. May be involved in cartilage development and in linking signal transduction pathways to the cytoskeleton.[UniProtKB:Q9HBL0]
== 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/gj/2gjy_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/main_output.php?pdb_ID=2gjy ConSurf].
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== Publication Abstract from PubMed ==
Tensin is a protein confined at those discrete and specialized regions of the plasma membrane, known as focal adhesions. It contains, at the C-terminus, a phosphotyrosine binding (PTB) domain that can interact with the cytoplasmic tail of beta-integrins and is necessary for localization of the protein to cell-matrix adhesions. Here, we present the NMR solution structure of the PTB domain of tensin1. Moreover, through NMR binding studies, we demonstrate that the PTB domain of tensin1 is able to interact with phosphatidylinositol 4, 5-diphosphate (PtIns(4,5)P2) and phosphatidylinositol 4-phosphate (PtIns(4)P), presenting higher affinity for the diphosphorylated inositide. Chemical shift mapping studies reveal a putative PtIns(4,5)P2 binding region that is distinct from the predicted integrin beta-tail recognition site. Heteronuclear NOE experiments, recorded in absence and presence of PtIns(4,5)P2, indicate that the interaction with lipids decreases the flexibility of loop regions, predicted to be important for integrin binding, and thus, proposes a possible correlation between the two distinct binding events. Therefore, our studies suggest that capture of lipids by the PTB domain of tensin1 may play a role for the protein function at focal adhesions.

The PTB domain of tensin: NMR solution structure and phosphoinositides binding studies.,Leone M, Yu EC, Liddington RC, Pasquale EB, Pellecchia M Biopolymers. 2008 Jan;89(1):86-92. PMID:17922498<ref>PMID:17922498</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Gallus gallus]]
[[Category: Large Structures]]
[[Category: Leone M]]
[[Category: Pellecchia M]]