1hci
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(New page: 200px<br /> <applet load="1hci" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hci, resolution 2.80Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:09, 12 November 2007
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CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ
Overview
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.
About this Structure
1HCI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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
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