2eyn: Difference between revisions
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==Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution== | ==Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution== | ||
<StructureSection load='2eyn' size='340' side='right' caption='[[2eyn]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='2eyn' size='340' side='right' caption='[[2eyn]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eyi|2eyi]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2eyi|2eyi]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTN1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACTN1 ([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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2eyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyn OCA], [http://pdbe.org/2eyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eyn RCSB], [http://www.ebi.ac.uk/pdbsum/2eyn PDBsum]</span></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=2eyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyn OCA], [http://pdbe.org/2eyn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2eyn RCSB], [http://www.ebi.ac.uk/pdbsum/2eyn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2eyn ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</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/ | </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=2eyn ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 2eyn" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2eyn" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:31, 18 October 2017
Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolutionCrystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution
Structural highlights
Function[ACTN1_HUMAN] F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAlpha-actinin belongs to the spectrin family of actin crosslinking and bundling proteins that function as key regulators of cell motility, morphology and adhesion. The actin-binding domain (ABD) of these proteins consists of two consecutive calponin homology (CH) domains. Electron microscopy studies on ABDs appear to support two competing actin-binding models, extended and compact, whereas the crystal structures typically display a compact conformation. We have determined the 1.7A resolution structure of the ABD of alpha-actinin 1, a ubiquitously expressed isoform. The structure displays the classical compact conformation. We evaluated the two binding models by surface conservation analysis. The results show a conserved surface that spans both domains and corresponds to two previously identified actin-binding sites (ABS2 and ABS3). A third, and probably less important site, ABS1, is mostly buried in the compact conformation. However, a thorough examination of existing structures suggests a weak and semi-polar binding interface between the two CHs, leaving open the possibility of domain reorientation or opening. Our results are consistent with a two-step binding mechanism in which the ABD interacts first in the compact form observed in the structures, and then transitions toward a higher affinity state, possibly through minor rearrangement of the domains. Crystal structure of the actin-binding domain of alpha-actinin 1: evaluating two competing actin-binding models.,Borrego-Diaz E, Kerff F, Lee SH, Ferron F, Li Y, Dominguez R J Struct Biol. 2006 Aug;155(2):230-8. Epub 2006 Apr 25. PMID:16698282[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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