1Z23

The serine-rich domain from Crk-associated substrate (p130Cas)

1Z23 の概要

• エントリーDOI: 10.2210/pdb1z23/pdb
• 分子名称: CRK-associated substrate (1 entity in total)
• 機能のキーワード: four-helix bundle, cell adhesion
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cell junction, focal adhesion: Q63767
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17348.47

構造登録者

Briknarova, K.,Nasertorabi, F.,Havert, M.L.,Eggleston, E.,Hoyt, D.W.,Li, C.,Olson, A.J.,Vuori, K.,Ely, K.R. (登録日: 2005-03-07, 公開日: 2005-04-05, 最終更新日: 2024-05-22)

主引用文献

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

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: 15795225
DOI: 10.1074/jbc.M501258200

実験手法

SOLUTION NMR