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2h0q

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(New page: 200px<br /><applet load="2h0q" size="350" color="white" frame="true" align="right" spinBox="true" caption="2h0q, resolution 1.82&Aring;" /> '''Crystal Structure of...)
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[[Image:2h0q.jpg|left|200px]]<br /><applet load="2h0q" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2h0q, resolution 1.82&Aring;" />
 
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'''Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1)'''<br />
 
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==Overview==
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==Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1)==
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Precise signaling by the T cell receptor (TCR) is crucial for a proper, immune response. To ensure that T cells respond appropriately to antigenic, stimuli, TCR signaling pathways are subject to multiple levels of, regulation. Sts-1 negatively regulates signaling pathways downstream of, the TCR by an unknown mechanism(s). Here, we demonstrate that Sts-1 is a, phosphatase that can target the tyrosine kinase Zap-70 among other, proteins. The X-ray structure of the Sts-1 C terminus reveals that it has, homology to members of the phosphoglycerate mutase/acid phosphatase, (PGM/AcP) family of enzymes, with residues known to be important for, PGM/AcP catalytic activity conserved in nature and position in Sts-1., Point mutations that impair Sts-1 phosphatase activity in vitro also, impair the ability of Sts-1 to regulate TCR signaling in T cells. These, observations reveal a PGM/AcP-like enzyme activity involved in the control, of antigen receptor signaling.
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<StructureSection load='2h0q' size='340' side='right'caption='[[2h0q]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[2h0q]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H0Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2H0Q FirstGlance]. <br>
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2H0Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H0Q OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.82&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2h0q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h0q OCA], [https://pdbe.org/2h0q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2h0q RCSB], [https://www.ebi.ac.uk/pdbsum/2h0q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2h0q ProSAT]</span></td></tr>
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==Reference==
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</table>
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A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling., Mikhailik A, Ford B, Keller J, Chen Y, Nassar N, Carpino N, Mol Cell. 2007 Aug 3;27(3):486-97. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17679096 17679096]
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== Function ==
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[https://www.uniprot.org/uniprot/UBS3B_MOUSE UBS3B_MOUSE] Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.<ref>PMID:14738763</ref> <ref>PMID:19733910</ref> <ref>PMID:20585042</ref> <ref>PMID:17679096</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h0/2h0q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2h0q ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
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[[Category: Single protein]]
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[[Category: Carpino N]]
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[[Category: Carpino, N.]]
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[[Category: Ford B]]
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[[Category: Ford, B.]]
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[[Category: Nassar N]]
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[[Category: Nassar, N.]]
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[[Category: pgm]]
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[[Category: signaling protein]]
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[[Category: sts-1]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:21:03 2008''
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Current revision

Crystal Structure of the PGM domain of the Suppressor of T-Cell receptor (Sts-1)

PDB ID 2h0q

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