The serine-rich domain from Crk-associated substrate ( p130cas) is a four-helix bundle.
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.[1]References
- The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle. Briknarová, K., Nasertorabi, F., Havert, M.L., Eggleston, E., Hoyt, D.W., Li, C., Olson, A.J., Vuori, K., Ely, K.R. J. Biol. Chem. (2005) [Pubmed]
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