1sjj

<StructureSection load='1sjj' size='340' side='right' caption='[[1sjj]], [[Resolution|resolution]] 20.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[1sjj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SJJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SJJ FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hci|1hci]], [[1aoa|1aoa]], [[1dxx|1dxx]], [[1qag|1qag]], [[1cfd|1cfd]]</td></tr>

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

[[http://www.uniprot.org/uniprot/ACTN1_CHICK ACTN1_CHICK]] F-actin cross-linking protein is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/sj/1sjj_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

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

== Publication Abstract from PubMed ==

Cryoelectron microscopy was used to obtain a 3-D image at 2.0 nm resolution of 2-D arrays of smooth muscle alpha-actinin. The reconstruction reveals a well-resolved long central domain with 90 degrees of left-handed twist and near 2-fold symmetry. However, the molecular ends which contain the actin binding and calmodulin-like domains, have different structures oriented approximately 90 degrees to each other. Atomic structures for the alpha-actinin domains were built by homology modeling and assembled into an atomic model. Model building suggests that in the 2-D arrays, the two calponin homology domains that comprise the actin-binding domain have a closed conformation at one end and an open conformation at the other end due to domain swapping. The open and closed conformations of the actin-binding domain suggests flexibility that may underlie Ca2+ regulation. The approximately 90 degrees orientation difference at the molecular ends may underlie alpha-actinin's ability to crosslink actin filaments in nearly any orientation.

A 3-D reconstruction of smooth muscle alpha-actinin by CryoEm reveals two different conformations at the actin-binding region.,Liu J, Taylor DW, Taylor KA J Mol Biol. 2004 Apr 16;338(1):115-25. PMID:15050827<ref>PMID:15050827</ref>

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

</div>

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

*[[Actinin|Actinin]]

[[Category: Chick]]

[[Category: Liu, J]]

[[Category: Taylor, D W]]

[[Category: Taylor, K A]]

[[Category: 3-helix bundle]]

[[Category: Contractile protein]]