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1z23

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(New page: 200px<br /><applet load="1z23" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z23" /> '''The serine-rich domain from Crk-associated s...)
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[[Image:1z23.gif|left|200px]]<br /><applet load="1z23" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1z23" />
 
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'''The serine-rich domain from Crk-associated substrate (p130Cas)'''<br />
 
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==Overview==
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==The serine-rich domain from Crk-associated substrate (p130Cas)==
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p130(cas) (Crk-associated substrate) is a docking protein that is involved, in assembly of focal adhesions and concomitant cellular signaling. It, plays a role in physiological regulation of cell adhesion, migration, survival, and proliferation, as well as in oncogenic transformation. The, molecule consists of multiple protein-protein interaction motifs, including a serine-rich region that is positioned between Crk and, Src-binding sites. This study reports the first structure of a functional, domain of Cas. The solution structure of the serine-rich region has been, determined by NMR spectroscopy, demonstrating that this is a stable domain, that folds as a four-helix bundle, a protein-interaction motif. The, serine-rich region bears strong structural similarity to four-helix, bundles found in other adhesion components like focal adhesion kinase, alpha-catenin, or vinculin. Potential sites for phosphorylation and, interaction with the 14-3-3 family of cellular regulators are identified, in the domain and characterized by site-directed mutagenesis and binding, assays. Mapping the degree of amino acid conservation onto the molecular, surface reveals a patch of invariant residues near the C terminus of the, bundle, which may represent a previously unidentified site for protein, interaction.
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<StructureSection load='1z23' size='340' side='right'caption='[[1z23]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1z23]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z23 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z23 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z23 OCA], [https://pdbe.org/1z23 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z23 RCSB], [https://www.ebi.ac.uk/pdbsum/1z23 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z23 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/BCAR1_RAT BCAR1_RAT] Appears to have a central function in transformation of some cell types.
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== Function ==
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[https://www.uniprot.org/uniprot/BCAR1_RAT BCAR1_RAT] Docking protein which plays a central coordinating role for tyrosine-kinase-based signaling related to cell adhesion. Implicated in induction of cell migration (By similarity).
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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/z2/1z23_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=1z23 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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p130(cas) (Crk-associated substrate) is a docking protein that is involved in assembly of focal adhesions and concomitant cellular signaling. It plays a role in physiological regulation of cell adhesion, migration, survival, and proliferation, as well as in oncogenic transformation. The molecule consists of multiple protein-protein interaction motifs, including a serine-rich region that is positioned between Crk and Src-binding sites. This study reports the first structure of a functional domain of Cas. The solution structure of the serine-rich region has been determined by NMR spectroscopy, demonstrating that this is a stable domain that folds as a four-helix bundle, a protein-interaction motif. The serine-rich region bears strong structural similarity to four-helix bundles found in other adhesion components like focal adhesion kinase, alpha-catenin, or vinculin. Potential sites for phosphorylation and interaction with the 14-3-3 family of cellular regulators are identified in the domain and characterized by site-directed mutagenesis and binding assays. Mapping the degree of amino acid conservation onto the molecular surface reveals a patch of invariant residues near the C terminus of the bundle, which may represent a previously unidentified site for protein interaction.
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==About this Structure==
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The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle.,Briknarova K, Nasertorabi F, Havert ML, Eggleston E, Hoyt DW, Li C, Olson AJ, Vuori K, Ely KR J Biol Chem. 2005 Jun 10;280(23):21908-14. Epub 2005 Mar 28. PMID:15795225<ref>PMID:15795225</ref>
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1Z23 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z23 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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The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle., Briknarova K, Nasertorabi F, Havert ML, Eggleston E, Hoyt DW, Li C, Olson AJ, Vuori K, Ely KR, J Biol Chem. 2005 Jun 10;280(23):21908-14. Epub 2005 Mar 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15795225 15795225]
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</div>
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<div class="pdbe-citations 1z23" 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>
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[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Briknarova K]]
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[[Category: Briknarova, K.]]
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[[Category: Eggleston E]]
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[[Category: Eggleston, E.]]
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[[Category: Ely KR]]
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[[Category: Ely, K.R.]]
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[[Category: Havert ML]]
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[[Category: Havert, M.L.]]
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[[Category: Hoyt DW]]
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[[Category: Hoyt, D.W.]]
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[[Category: Li C]]
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[[Category: Li, C.]]
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[[Category: Nasertorabi F]]
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[[Category: Nasertorabi, F.]]
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[[Category: Olson AJ]]
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[[Category: Olson, A.J.]]
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[[Category: Vuori K]]
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[[Category: Vuori, K.]]
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[[Category: four-helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:12:03 2007''
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Current revision

The serine-rich domain from Crk-associated substrate (p130Cas)

PDB ID 1z23

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