1hci
From Proteopedia
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| - | [[Image:1hci.gif|left|200px]] | + | [[Image:1hci.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ''' | + | {{Structure |
| + | |PDB= 1hci |SIZE=350|CAPTION= <scene name='initialview01'>1hci</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HCI is a [ | + | 1HCI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCI OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11470434 11470434] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: z-line]] | [[Category: z-line]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:15 2008'' |
Revision as of 09:35, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 11:35:15 2008
