1Z23
The serine-rich domain from Crk-associated substrate (p130Cas)
Summary for 1Z23
| Entry DOI | 10.2210/pdb1z23/pdb |
| Descriptor | CRK-associated substrate (1 entity in total) |
| Functional Keywords | four-helix bundle, cell adhesion |
| Biological source | Rattus norvegicus (Norway rat) |
| Cellular location | Cell junction, focal adhesion: Q63767 |
| Total number of polymer chains | 1 |
| Total formula weight | 17348.47 |
| Authors | Briknarova, K.,Nasertorabi, F.,Havert, M.L.,Eggleston, E.,Hoyt, D.W.,Li, C.,Olson, A.J.,Vuori, K.,Ely, K.R. (deposition date: 2005-03-07, release date: 2005-04-05, Last modification date: 2024-05-22) |
| Primary citation | Briknarova, K.,Nasertorabi, F.,Havert, M.L.,Eggleston, E.,Hoyt, D.W.,Li, C.,Olson, A.J.,Vuori, K.,Ely, K.R. The serine-rich domain from Crk-associated substrate (p130cas) is a four-helix bundle. J.Biol.Chem., 280:21908-21914, 2005 Cited by PubMed Abstract: 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. PubMed: 15795225DOI: 10.1074/jbc.M501258200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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