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2fci

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Revision as of 09:04, 14 June 2018

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

Structural highlights

2fci is a 2 chain structure with sequence from Bovin. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	, ,
Gene:	PLCG1 (BOVIN)
Activity:	Phosphoinositide phospholipase C, with EC number 3.1.4.11
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PLCG1_BOVIN] Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, FGFR1, FGFR2, FGFR3 and FGFR4. Plays a role in actin reorganization and cell migration (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Groesch TD, Zhou F, Mattila S, Geahlen RL, Post CB. Structural basis for the requirement of two phosphotyrosine residues in signaling mediated by Syk tyrosine kinase. J Mol Biol. 2006 Mar 10;356(5):1222-36. Epub 2005 Dec 27. PMID:16410013 doi:10.1016/j.jmb.2005.11.095

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2fci"

@@ Line 1: / Line 1: @@
 ==Structural basis for the requirement of two phosphotyrosines in signaling mediated by Syk tyrosine kinase==
 <StructureSection load='2fci' size='340' side='right' caption='[[2fci]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PLCG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoinositide_phospholipase_C Phosphoinositide phospholipase C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.11 3.1.4.11] </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=2fci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fci OCA], [http://pdbe.org/2fci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fci RCSB], [http://www.ebi.ac.uk/pdbsum/2fci PDBsum]</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=2fci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fci OCA], [http://pdbe.org/2fci PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2fci RCSB], [http://www.ebi.ac.uk/pdbsum/2fci PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2fci ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/2fci_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fc/2fci_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].
+</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].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

2fci

From Proteopedia

Revision as of 09:04, 14 June 2018

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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