1wku

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[[Image:1wku.gif|left|200px]]
[[Image:1wku.gif|left|200px]]
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{{Structure
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|PDB= 1wku |SIZE=350|CAPTION= <scene name='initialview01'>1wku</scene>, resolution 1.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1wku", creates the "Structure Box" on the page.
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|GENE= ACTN3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|DOMAIN=
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{{STRUCTURE_1wku| PDB=1wku | SCENE= }}
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|RELATEDENTRY=[[1aoa|1AOA]], [[1dxx|1DXX]], [[1mb8|1MB8]], [[1qag|1QAG]], [[1tjt|1TJT]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1wku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wku OCA], [http://www.ebi.ac.uk/pdbsum/1wku PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1wku RCSB]</span>
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'''High resolution structure of the human alpha-actinin isoform 3'''
'''High resolution structure of the human alpha-actinin isoform 3'''
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[[Category: Gautel, M.]]
[[Category: Gautel, M.]]
[[Category: Sjoblom, B.]]
[[Category: Sjoblom, B.]]
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[[Category: actin binding domain]]
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[[Category: Actin binding domain]]
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[[Category: calponin homology domain]]
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[[Category: Calponin homology domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:49:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:37:34 2008''
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Revision as of 10:49, 3 May 2008

Template:STRUCTURE 1wku

High resolution structure of the human alpha-actinin isoform 3


Contents

Overview

Alpha-actinin is the major F-actin crosslinking protein in both muscle and non-muscle cells. We report the crystal structure of the actin binding domain of human muscle alpha-actinin-3, which is formed by two consecutive calponin homology domains arranged in a "closed" conformation. Structural studies and available biochemical data on actin binding domains suggest that two calponin homology domains come in a closed conformation in the native apo-form, and that conformational changes involving the relative orientation of the two calponin homology domains are required for efficient binding to actin filaments. The actin binding activity of muscle isoforms is supposed to be regulated by phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), which binds to the second calponin homology domain. On the basis of structural analysis we propose a distinct binding site for PtdIns(4,5)P2, where the fatty acid moiety would be oriented in a direction that allows it to interact with the linker sequence between the actin binding domain and the first spectrin-like repeat, regulating thereby the binding of the C-terminal calmodulin-like domain to this linker.

Disease

Known disease associated with this structure: Alpha-actinin-3 deficiency OMIM:[102574], Sprinting performance OMIM:[102574]

About this Structure

1WKU is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of the actin binding domain from alpha-actinin in its closed conformation: structural insight into phospholipid regulation of alpha-actinin., Franzot G, Sjoblom B, Gautel M, Djinovic Carugo K, J Mol Biol. 2005 Apr 22;348(1):151-65. PMID:15808860 Page seeded by OCA on Sat May 3 13:49:07 2008

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