1z23: Difference between revisions
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< | ==The serine-rich domain from Crk-associated substrate (p130Cas)== | ||
<StructureSection load='1z23' size='340' side='right'caption='[[1z23]]' scene=''> | |||
You may | == Structural highlights == | ||
<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> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
-- | <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> | ||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/BCAR1_RAT BCAR1_RAT] Appears to have a central function in transformation of some cell types. | |||
== Function == | |||
[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). | |||
== 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/z2/1z23_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=1z23 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1z23" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Briknarova | [[Category: Briknarova K]] | ||
[[Category: Eggleston | [[Category: Eggleston E]] | ||
[[Category: Ely | [[Category: Ely KR]] | ||
[[Category: Havert | [[Category: Havert ML]] | ||
[[Category: Hoyt | [[Category: Hoyt DW]] | ||
[[Category: Li | [[Category: Li C]] | ||
[[Category: Nasertorabi | [[Category: Nasertorabi F]] | ||
[[Category: Olson | [[Category: Olson AJ]] | ||
[[Category: Vuori | [[Category: Vuori K]] | ||
Latest revision as of 08:08, 15 May 2024
The serine-rich domain from Crk-associated substrate (p130Cas)
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