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|1hci, resolution 2.80Å ()|
CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ
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.
Crystal structure of the alpha-actinin rod reveals an extensive torsional twist., Ylanne J, Scheffzek K, Young P, Saraste M, Structure. 2001 Jul 3;9(7):597-604. PMID:11470434
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- Ylanne J, Scheffzek K, Young P, Saraste M. Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure. 2001 Jul 3;9(7):597-604. PMID:11470434