The BioGRID | PUBLICATION VIEW

	Structure (Camb.) Jul (2001); 9(7):597-604
Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.
Ylanne J, Scheffzek K, Young P, Saraste M
European Molecular Biology Laboratory, EMBL, Structural and Computational Biology Programme, Meyerhofstrasse 1, D-69117, Heidelberg, Germany. ylanne@embl-heidelberg.de
Abstract: BACKGROUND: Alpha-actinin is a ubiquitously expressed protein found in numerous actin structures. It consists of an N-terminal actin binding domain, a central rod domain, and a C-terminal domain and functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins. RESULTS: We report here the crystal structure of the alpha-actinin rod. The structure is a twisted antiparallel dimer that contains a conserved acidic surface. CONCLUSIONS: The novel features revealed by the structure allow prediction of the orientation of parallel and antiparallel cross-linked actin filaments in relation to alpha-actinin. The conserved acidic surface is a possible interaction site for several cytoplasmic tails of transmembrane proteins involved in the recruitment of alpha-actinin to the plasma membrane.
[PUBMED: 11470434]