June 10, 2005
Journal Article

The Serine-rich Domain from Crk-associated Substrate (p130Cas) is a Four-helix Bundle

Abstract

p130Cas (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 nuclear magnetic resonance spectroscopy (NMR) demonstrating that this is a stable domain that folds as a four-helix bundle, a protein-interaction motif.

Revised: September 29, 2005 | Published: June 10, 2005

Citation

Briknarova K., F. Nasertorabi, M.L. Havert, E. Eggleston, D.W. Hoyt, C. Li, and A.J. Olson, et al. 2005. The Serine-rich Domain from Crk-associated Substrate (p130Cas) is a Four-helix Bundle. Journal of Biological Chemistry 280, no. 23:21908-21914. PNNL-SA-45324.