1z23

From Proteopedia

(Difference between revisions)

Revision as of 20:56, 10 September 2015

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

Structural highlights

1z23 is a 1 chain structure with sequence from Buffalo rat. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Disease

[BCAR1_RAT] Appears to have a central function in transformation of some cell types.

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Briknarova K, Nasertorabi F, Havert ML, Eggleston E, Hoyt DW, Li C, Olson AJ, Vuori K, Ely KR. The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle. J Biol Chem. 2005 Jun 10;280(23):21908-14. Epub 2005 Mar 28. PMID:15795225 doi:10.1074/jbc.M501258200

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z23"

@@ Line 2: / Line 2: @@
 <StructureSection load='1z23' size='340' side='right' caption='[[1z23]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z23]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z23 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z23]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Z23 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z23 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1z23 RCSB], [http://www.ebi.ac.uk/pdbsum/1z23 PDBsum]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z23 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z23 OCA], [http://pdbe.org/1z23 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z23 RCSB], [http://www.ebi.ac.uk/pdbsum/1z23 PDBsum]</span></td></tr>
 </table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/BCAR1_RAT BCAR1_RAT]] Appears to have a central function in transformation of some cell types.
+== Function ==
+[[http://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]]
@@ Line 23: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, 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: Rattus norvegicus]]
+[[Category: Buffalo rat]]
 [[Category: Briknarova, K]]
 [[Category: Eggleston, E]]

1z23

From Proteopedia

Revision as of 20:56, 10 September 2015

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

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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