2fci

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(New page: 200px<br /><applet load="2fci" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fci" /> '''Structural basis for the requirement of two ...)
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[[Image:2fci.gif|left|200px]]<br /><applet load="2fci" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2fci" />
 
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'''Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase'''<br />
 
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==Overview==
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==Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase==
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The protein-tyrosine kinase Syk couples immune recognition receptors to, multiple signal transduction pathways, including the mobilization of, calcium and the activation of NFAT. The ability of Syk to regulate, signaling is influenced by its phosphorylation on tyrosine residues within, the linker B region. The phosphorylation of both Y342 and Y346 is, necessary for optimal signaling from the B cell receptor for antigen. The, SH2 domains of multiple signaling proteins share the ability to bind this, doubly phosphorylated site. The NMR structure of the C-terminal SH2 domain, of PLCgamma (PLCC) bound to a doubly phosphorylated Syk peptide reveals a, novel mode of phosphotyrosine recognition. PLCC undergoes extensive, conformational changes upon binding to form a second, phosphotyrosine-binding pocket in which pY346 is largely desolvated and, stabilized through electrostatic interactions. The formation of the second, binding pocket is distinct from other modes of phosphotyrosine recognition, in SH2-protein association. The dependence of signaling on simultaneous, phosphorylation of these two tyrosine residues offers a new mechanism to, fine-tune the cellular response to external stimulation.
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<StructureSection load='2fci' size='340' side='right'caption='[[2fci]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2fci]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FCI FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=GMA:4-AMIDO-4-CARBAMOYL-BUTYRIC+ACID'>GMA</scene>, <scene name='pdbligand=PTR:O-PHOSPHOTYROSINE'>PTR</scene></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=2fci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fci OCA], [https://pdbe.org/2fci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fci RCSB], [https://www.ebi.ac.uk/pdbsum/2fci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fci ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q32PK0_BOVIN Q32PK0_BOVIN]
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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/fc/2fci_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=2fci ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The protein-tyrosine kinase Syk couples immune recognition receptors to multiple signal transduction pathways, including the mobilization of calcium and the activation of NFAT. The ability of Syk to regulate signaling is influenced by its phosphorylation on tyrosine residues within the linker B region. The phosphorylation of both Y342 and Y346 is necessary for optimal signaling from the B cell receptor for antigen. The SH2 domains of multiple signaling proteins share the ability to bind this doubly phosphorylated site. The NMR structure of the C-terminal SH2 domain of PLCgamma (PLCC) bound to a doubly phosphorylated Syk peptide reveals a novel mode of phosphotyrosine recognition. PLCC undergoes extensive conformational changes upon binding to form a second phosphotyrosine-binding pocket in which pY346 is largely desolvated and stabilized through electrostatic interactions. The formation of the second binding pocket is distinct from other modes of phosphotyrosine recognition in SH2-protein association. The dependence of signaling on simultaneous phosphorylation of these two tyrosine residues offers a new mechanism to fine-tune the cellular response to external stimulation.
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==About this Structure==
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Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by Syk tyrosine kinase.,Groesch TD, Zhou F, Mattila S, Geahlen RL, Post CB J Mol Biol. 2006 Mar 10;356(5):1222-36. Epub 2005 Dec 27. PMID:16410013<ref>PMID:16410013</ref>
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2FCI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with ACE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FCI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by Syk tyrosine kinase., Groesch TD, Zhou F, Mattila S, Geahlen RL, Post CB, J Mol Biol. 2006 Mar 10;356(5):1222-36. Epub 2005 Dec 27. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16410013 16410013]
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</div>
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<div class="pdbe-citations 2fci" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Transferase]]
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[[Category: Geahlen RL]]
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[[Category: Geahlen, R.L.]]
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[[Category: Groesch TD]]
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[[Category: Groesch, T.D.]]
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[[Category: Mattila S]]
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[[Category: Mattila, S.]]
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[[Category: Post CB]]
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[[Category: Post, C.B.]]
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[[Category: Zhou F]]
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[[Category: Zhou, F.]]
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[[Category: ACE]]
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[[Category: phosphopeptide]]
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[[Category: plcc]]
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[[Category: plcgamma]]
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[[Category: sh2 domain]]
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[[Category: syk kinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:28:57 2007''
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Current revision

Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase

PDB ID 2fci

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