1u5s

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{{Seed}}
 
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[[Image:1u5s.png|left|200px]]
 
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==NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain==
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The line below this paragraph, containing "STRUCTURE_1u5s", creates the "Structure Box" on the page.
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<StructureSection load='1u5s' size='340' side='right'caption='[[1u5s]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1u5s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1U5S FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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=ZN:ZINC+ION'>ZN</scene></td></tr>
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{{STRUCTURE_1u5s| PDB=1u5s | SCENE= }}
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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=1u5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1u5s OCA], [https://pdbe.org/1u5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1u5s RCSB], [https://www.ebi.ac.uk/pdbsum/1u5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1u5s ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/NCK2_HUMAN NCK2_HUMAN] Adapter protein which associates with tyrosine-phosphorylated growth factor receptors or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in ELK1-dependent transcriptional activation in response to activated Ras signaling.<ref>PMID:10026169</ref> <ref>PMID:16835242</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/u5/1u5s_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=1u5s 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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Weak protein-protein interactions (PPIs) (K(D) &gt; 10(-6) M) are critical determinants of many biological processes. However, in contrast to a large growing number of well-characterized, strong PPIs, the weak PPIs, especially those with K(D) &gt; 10(-4) M, are poorly explored. Genome wide, there exist few 3D structures of weak PPIs with K(D) &gt; 10(-4) M, and none with K(D) &gt; 10(-3) M. Here, we report the NMR structure of an extremely weak focal adhesion complex (K(D) approximately 3 x 10(-3) M) between Nck-2 SH3 domain and PINCH-1 LIM4 domain. The structure exhibits a remarkably small and polar interface with distinct binding modes for both SH3 and LIM domains. Such an interface suggests a transient Nck-2/PINCH-1 association process that may trigger rapid focal adhesion turnover during integrin signaling. Genetic rescue experiments demonstrate that this interface is indeed involved in mediating cell shape change and migration. Together, the data provide a molecular basis for an ultraweak PPI in regulating focal adhesion dynamics during integrin signaling.
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===NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain===
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Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility.,Vaynberg J, Fukuda T, Chen K, Vinogradova O, Velyvis A, Tu Y, Ng L, Wu C, Qin J Mol Cell. 2005 Feb 18;17(4):513-23. PMID:15721255<ref>PMID:15721255</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_15721255}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1u5s" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 15721255 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_15721255}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1U5S is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5S OCA].
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==Reference==
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<ref group="xtra">PMID:15721255</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Fukuda, T.]]
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[[Category: Large Structures]]
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[[Category: Ng, L.]]
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[[Category: Fukuda T]]
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[[Category: Qin, J.]]
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[[Category: Ng L]]
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[[Category: Vaynberg, J.]]
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[[Category: Qin J]]
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[[Category: Velyvis, A.]]
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[[Category: Vaynberg J]]
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[[Category: Vinogradova, O.]]
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[[Category: Velyvis A]]
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[[Category: Wu, C.]]
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[[Category: Vinogradova O]]
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[[Category: Beta barrel]]
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[[Category: Wu C]]
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[[Category: Beta sheet]]
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[[Category: Protein-protein complex]]
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[[Category: Zinc finger]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 16:51:10 2009''
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Current revision

NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain

PDB ID 1u5s

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