1hci
From Proteopedia
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'''CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ''' | '''CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ''' | ||
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[[Category: Ylanne, J.]] | [[Category: Ylanne, J.]] | ||
[[Category: Young, P.]] | [[Category: Young, P.]] | ||
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| - | [[Category: | + | [[Category: Triple-helix coiled coil]] |
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| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:41:55 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 15:41, 2 May 2008
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 Page seeded by OCA on Fri May 2 18:41:55 2008
