2eyn: Difference between revisions

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-{{Seed}}
-[[Image:2eyn.png|left|200px]]
-<!--
+==Crystal structure of the actin-binding domain of human alpha-actinin 1 at 1.8 Angstrom resolution==
-The line below this paragraph, containing "STRUCTURE_2eyn", creates the "Structure Box" on the page.
+<StructureSection load='2eyn' size='340' side='right'caption='[[2eyn]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2eyn]] is a 1 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=2EYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EYN FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2eyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2eyn OCA], [https://pdbe.org/2eyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2eyn RCSB], [https://www.ebi.ac.uk/pdbsum/2eyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2eyn ProSAT]</span></td></tr>
-{{STRUCTURE_2eyn|  PDB=2eyn  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ACTN1_HUMAN 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 ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ey/2eyn_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=2eyn ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Alpha-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 human alpha-actinin 1 at 1.8 Angstrom resolution===
+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<ref>PMID:16698282</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2eyn" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16698282}}, adds the Publication Abstract to the page
+*[[Actinin 3D structures|Actinin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16698282 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16698282}}
+__TOC__
+</StructureSection>
-==About this Structure==
-EYN is a 1 chain 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=2EYN OCA].
-==Reference==
-<ref group="xtra">PMID:16698282</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Borrego-Diaz, E.]]
+[[Category: Large Structures]]
-[[Category: Dominguez, R.]]
+[[Category: Borrego-Diaz E]]
-[[Category: Ferron, F.]]
+[[Category: Dominguez R]]
-[[Category: Kerff, F.]]
+[[Category: Ferron F]]
-[[Category: Lee, S H.]]
+[[Category: Kerff F]]
-[[Category: Li, Y.]]
+[[Category: Lee SH]]
-[[Category: Actin-binding]]
+[[Category: Li Y]]
-[[Category: Actin-bundling]]
-[[Category: Actin-crosslinking]]
-[[Category: Calponin homology domain]]
-[[Category: Ch domain]]
-[[Category: Structural protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 18 10:11:50 2009''