1wku

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[[Image:1wku.gif|left|200px]]
 
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{{Structure
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==High resolution structure of the human alpha-actinin isoform 3==
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|PDB= 1wku |SIZE=350|CAPTION= <scene name='initialview01'>1wku</scene>, resolution 1.60&Aring;
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<StructureSection load='1wku' size='340' side='right'caption='[[1wku]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1wku]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WKU FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wku OCA], [https://pdbe.org/1wku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wku RCSB], [https://www.ebi.ac.uk/pdbsum/1wku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wku ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1aoa|1AOA]], [[1dxx|1DXX]], [[1mb8|1MB8]], [[1qag|1QAG]], [[1tjt|1TJT]]
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== Function ==
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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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[https://www.uniprot.org/uniprot/ACTN3_HUMAN ACTN3_HUMAN] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wk/1wku_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1wku ConSurf].
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<div style="clear:both"></div>
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'''High resolution structure of the human alpha-actinin isoform 3'''
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==See Also==
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*[[Actinin 3D structures|Actinin 3D structures]]
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*[[Parvin|Parvin]]
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==Overview==
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__TOC__
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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.
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</StructureSection>
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==Disease==
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Known disease associated with this structure: Alpha-actinin-3 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=102574 102574]], Sprinting performance OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=102574 102574]]
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==About this Structure==
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1WKU 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=1WKU OCA].
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15808860 15808860]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Carugo, K Djinovic.]]
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[[Category: Djinovic Carugo K]]
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[[Category: Franzot, G.]]
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[[Category: Franzot G]]
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[[Category: Gautel, M.]]
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[[Category: Gautel M]]
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[[Category: Sjoblom, B.]]
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[[Category: Sjoblom B]]
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[[Category: actin binding domain]]
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[[Category: calponin homology domain]]
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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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Current revision

High resolution structure of the human alpha-actinin isoform 3

PDB ID 1wku

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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