1z23
From Proteopedia
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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
Page seeded by OCA on Wed Nov 21 07:12:03 2007
