Display Settings:

Format

Send to:

Choose Destination
See comment in PubMed Commons below
Structure. 2001 Jul 3;9(7):597-604.

Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.

Author information

  • 1European 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.

PMID:
11470434
[PubMed - indexed for MEDLINE]
Free full text
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Icon for Elsevier Science
    Loading ...
    Write to the Help Desk