2ci8: Difference between revisions

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-{{Seed}}
-[[Image:2ci8.png|left|200px]]
-<!--
+==sh2 domain of human nck1 adaptor protein - uncomplexed==
-The line below this paragraph, containing "STRUCTURE_2ci8", creates the "Structure Box" on the page.
+<StructureSection load='2ci8' size='340' side='right'caption='[[2ci8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2ci8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CI8 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-{{STRUCTURE_2ci8|  PDB=2ci8  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ci8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ci8 OCA], [https://pdbe.org/2ci8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ci8 RCSB], [https://www.ebi.ac.uk/pdbsum/2ci8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ci8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/NCK1_HUMAN NCK1_HUMAN] Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ATM/ATR, but for efficient activation of downstream effectors, such as that of CHEK2. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling.<ref>PMID:10026169</ref> <ref>PMID:16835242</ref> <ref>PMID:17803907</ref>
+== 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/ci/2ci8_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=2ci8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Nck proteins are essential Src homology (SH) 2 and SH3 domain-bearing adapters that modulate actin cytoskeleton dynamics by linking proline-rich effector molecules to tyrosine kinases or phosphorylated signaling intermediates. Two mammalian pathogens, enteropathogenic Escherichia coli and vaccinia virus, exploit Nck as part of their infection strategy. Conflicting data indicate potential differences in the recognition specificities of the SH2 domains of the isoproteins Nck1 (Nckalpha) and Nck2 (Nckbeta and Grb4). We have characterized the binding specificities of both SH2 domains and find them to be essentially indistinguishable. Crystal structures of both domains in complex with phosphopeptides derived from the enteropathogenic E. coli protein Tir concur in identifying highly conserved, specific recognition of the phosphopeptide. Differential peptide recognition can therefore not account for the preference of either Nck in particular signaling pathways. Binding studies using sequentially mutated, high affinity phosphopeptides establish the sequence variability tolerated in peptide recognition. Based on this binding motif, we identify potential new binding partners of Nck1 and Nck2 and confirm this experimentally for the Arf-GAP GIT1.
-===SH2 DOMAIN OF HUMAN NCK1 ADAPTOR PROTEIN- UNCOMPLEXED===
+The phosphotyrosine peptide binding specificity of Nck1 and Nck2 Src homology 2 domains.,Frese S, Schubert WD, Findeis AC, Marquardt T, Roske YS, Stradal TE, Heinz DW J Biol Chem. 2006 Jun 30;281(26):18236-45. Epub 2006 Apr 24. PMID:16636066<ref>PMID:16636066</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_16636066}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 2ci8" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 16636066 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16636066}}
+__TOC__
+</StructureSection>
-==About this Structure==
-CI8 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CI8 OCA].
-==Reference==
-<ref group="xtra">PMID:16636066</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Findeis, A C.]]
+[[Category: Large Structures]]
-[[Category: Frese, S.]]
+[[Category: Findeis AC]]
-[[Category: Heinz, D W.]]
+[[Category: Frese S]]
-[[Category: Marquardt, T.]]
+[[Category: Heinz DW]]
-[[Category: Roske, Y S.]]
+[[Category: Marquardt T]]
-[[Category: Schubert, W D.]]
+[[Category: Roske YS]]
-[[Category: Stradal, T E.B.]]
+[[Category: Schubert W-D]]
-[[Category: Binding specificity]]
+[[Category: Stradal TEB]]
-[[Category: Host-pathogen]]
-[[Category: Interaction]]
-[[Category: Phosphorylation]]
-[[Category: Sh2-domain]]
-[[Category: Sh3 domain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 20:06:28 2009''