1z23
From Proteopedia
(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=" | + | [[Image:1z23.gif|left|200px]]<br /><applet load="1z23" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z23" /> | caption="1z23" /> | ||
'''The serine-rich domain from Crk-associated substrate (p130Cas)'''<br /> | '''The serine-rich domain from Crk-associated substrate (p130Cas)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | p130(cas) (Crk-associated substrate) is a docking protein that is involved | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z23 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Briknarova, K.]] | [[Category: Briknarova, K.]] | ||
[[Category: Eggleston, E.]] | [[Category: Eggleston, E.]] | ||
| - | [[Category: Ely, K | + | [[Category: Ely, K R.]] |
| - | [[Category: Havert, M | + | [[Category: Havert, M L.]] |
| - | [[Category: Hoyt, D | + | [[Category: Hoyt, D W.]] |
[[Category: Li, C.]] | [[Category: Li, C.]] | ||
[[Category: Nasertorabi, F.]] | [[Category: Nasertorabi, F.]] | ||
| - | [[Category: Olson, A | + | [[Category: Olson, A J.]] |
[[Category: Vuori, K.]] | [[Category: Vuori, K.]] | ||
[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:11:23 2008'' |
Revision as of 14:11, 21 February 2008
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The serine-rich domain from Crk-associated substrate (p130Cas)
Overview
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.
About this Structure
1Z23 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
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
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