1wku

<table><tr><td colspan='2'>[[1wku]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1WKU FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aoa|1aoa]], [[1dxx|1dxx]], [[1mb8|1mb8]], [[1qag|1qag]], [[1tjt|1tjt]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTN3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1wku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wku OCA], [http://pdbe.org/1wku PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wku RCSB], [http://www.ebi.ac.uk/pdbsum/1wku PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wku ProSAT]</span></td></tr>

[[http://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.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

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.

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<ref>PMID:15808860</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1wku" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Carugo, K Djinovic]]

[[Category: Franzot, G]]

[[Category: Gautel, M]]

[[Category: Sjoblom, B]]

[[Category: Contractile protein]]