1z23
From Proteopedia
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| - | [[Image:1z23.gif|left|200px]] | + | [[Image:1z23.gif|left|200px]] |
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| - | '''The serine-rich domain from Crk-associated substrate (p130Cas)''' | + | {{Structure |
| + | |PDB= 1z23 |SIZE=350|CAPTION= <scene name='initialview01'>1z23</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''The serine-rich domain from Crk-associated substrate (p130Cas)''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1Z23 is a [ | + | 1Z23 is a [[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== | ||
| - | 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:// | + | 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://www.ncbi.nlm.nih.gov/pubmed/15795225 15795225] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: four-helix bundle]] | [[Category: four-helix bundle]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:30:21 2008'' |
Revision as of 13:30, 20 March 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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