1u5s

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[[Image:1u5s.gif|left|200px]]<br /><applet load="1u5s" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1u5s" />
 
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'''NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain'''<br />
 
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==Overview==
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==NMR structure of the complex between Nck-2 SH3 domain and PINCH-1 LIM4 domain==
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<StructureSection load='1u5s' size='340' side='right'caption='[[1u5s]]' scene=''>
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== Structural highlights ==
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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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</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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<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 ==
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.
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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==About this Structure==
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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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1U5S is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U5S 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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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15721255 15721255]
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</div>
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<div class="pdbe-citations 1u5s" 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: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Fukuda, T.]]
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[[Category: Fukuda T]]
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[[Category: Ng, L.]]
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[[Category: Ng L]]
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[[Category: Qin, J.]]
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[[Category: Qin J]]
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[[Category: Vaynberg, J.]]
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[[Category: Vaynberg J]]
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[[Category: Velyvis, A.]]
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[[Category: Velyvis A]]
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[[Category: Vinogradova, O.]]
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[[Category: Vinogradova O]]
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[[Category: Wu, C.]]
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[[Category: Wu C]]
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[[Category: ZN]]
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[[Category: beta barrel]]
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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 Thu Feb 21 15:20:57 2008''
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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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