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=''> | |||
== 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> | |||
</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 11:08, 15 May 2024
The serine-rich domain from Crk-associated substrate (p130Cas)The serine-rich domain from Crk-associated substrate (p130Cas)
Structural highlights
DiseaseBCAR1_RAT Appears to have a central function in transformation of some cell types. FunctionBCAR1_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedp130(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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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