Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.
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.
Mesh Terms:
Actinin, Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Escherichia coli, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Recombinant Proteins
Actinin, Amino Acid Sequence, Crystallography, X-Ray, Dimerization, Escherichia coli, Humans, Models, Molecular, Molecular Sequence Data, Protein Conformation, Recombinant Proteins
Structure
Date: Jul. 03, 2001
PubMed ID: 11470434
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