The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle.

摘要: Abstract p130cas (Crk-associated substrate) is a docking protein that involved in assembly of focal adhesions and concomitant cellular signaling. It plays role physiological regulation cell adhesion, migration, survival, proliferation, as well oncogenic transformation. The molecule consists multiple protein-protein interaction motifs, including serine-rich region positioned between Crk Src-binding sites. This study reports the first structure functional domain Cas. solution has been determined by NMR spectroscopy, demonstrating this stable folds four-helix bundle, protein-interaction motif. bears strong structural similarity to bundles found other adhesion components like kinase, α-catenin, or vinculin. Potential sites for phosphorylation with 14-3-3 family regulators are identified characterized site-directed mutagenesis binding assays. Mapping degree amino acid conservation onto molecular surface reveals patch invariant residues near C terminus which may represent previously unidentified site interaction.