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1hci
From Proteopedia
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| - | [[Image:1hci.gif|left|200px]] | ||
| - | + | ==CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ== | |
| - | + | <StructureSection load='1hci' size='340' side='right'caption='[[1hci]], [[Resolution|resolution]] 2.80Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1hci]] 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=1HCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HCI FirstGlance]. <br> | |
| - | | | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=1hci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hci OCA], [https://pdbe.org/1hci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hci RCSB], [https://www.ebi.ac.uk/pdbsum/1hci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hci ProSAT]</span></td></tr> |
| - | + | </table> | |
| + | == Disease == | ||
| + | [https://www.uniprot.org/uniprot/ACTN2_HUMAN ACTN2_HUMAN] Defects in ACTN2 are the cause of cardiomyopathy dilated type 1AA (CMD1AA) [MIM:[https://omim.org/entry/612158 612158]. Dilated cardiomyopathy is a disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.<ref>PMID:14567970</ref> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACTN2_HUMAN ACTN2_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/hc/1hci_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=1hci ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BACKGROUND: Alpha-actinin is a ubiquitously expressed protein found in numerous actin structures. It consists of an N-terminal actin binding domain, a central rod domain, and a C-terminal domain and functions as a homodimer to cross-link actin filaments. The rod domain determines the distance between cross-linked actin filaments and also serves as an interaction site for several cytoskeletal and signaling proteins. RESULTS: We report here the crystal structure of the alpha-actinin rod. The structure is a twisted antiparallel dimer that contains a conserved acidic surface. CONCLUSIONS: The novel features revealed by the structure allow prediction of the orientation of parallel and antiparallel cross-linked actin filaments in relation to alpha-actinin. The conserved acidic surface is a possible interaction site for several cytoplasmic tails of transmembrane proteins involved in the recruitment of alpha-actinin to the plasma membrane. | ||
| - | + | Crystal structure of the alpha-actinin rod reveals an extensive torsional twist.,Ylanne J, Scheffzek K, Young P, Saraste M Structure. 2001 Jul 3;9(7):597-604. PMID:11470434<ref>PMID:11470434</ref> | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 1hci" style="background-color:#fffaf0;"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Actinin 3D structures|Actinin 3D structures]] | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | |
| - | + | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Saraste | + | [[Category: Saraste M]] |
| - | [[Category: Scheffzek | + | [[Category: Scheffzek K]] |
| - | [[Category: Ylanne | + | [[Category: Ylanne J]] |
| - | [[Category: Young | + | [[Category: Young P]] |
| - | [[Category: | + | [[Category: Z-disk]] |
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Current revision
CRYSTAL STRUCTURE OF THE ROD DOMAIN OF ALPHA-ACTININ
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Categories: Homo sapiens | Large Structures | Saraste M | Scheffzek K | Ylanne J | Young P | Z-disk
