1quu

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[[Image:1quu.gif|left|200px]]
 
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{{Structure
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==CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ==
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|PDB= 1quu |SIZE=350|CAPTION= <scene name='initialview01'>1quu</scene>, resolution 2.5&Aring;
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<StructureSection load='1quu' size='340' side='right'caption='[[1quu]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1quu]] 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=1QUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUU FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1quu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1quu OCA], [https://pdbe.org/1quu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1quu RCSB], [https://www.ebi.ac.uk/pdbsum/1quu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1quu ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Disease ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1quu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1quu OCA], [http://www.ebi.ac.uk/pdbsum/1quu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1quu RCSB]</span>
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[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>
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}}
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qu/1quu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1quu ConSurf].
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<div style="clear:both"></div>
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'''CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ'''
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==See Also==
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*[[Actinin 3D structures|Actinin 3D structures]]
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== References ==
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==Overview==
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<references/>
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We have determined the crystal structure of the two central repeats in the alpha-actinin rod at 2.5 A resolution. The repeats are connected by a helical linker and form a symmetric, antiparallel dimer in which the repeats are aligned rather than staggered. Using this structure, which reveals the structural principle that governs the architecture of alpha-actinin, we have devised a plausible model of the entire alpha-actinin rod. The electrostatic properties explain how the two alpha-actinin subunits assemble in an antiparallel fashion, placing the actin-binding sites at both ends of the rod. This molecular architecture results in a protein that is able to form cross-links between actin filaments.
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__TOC__
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</StructureSection>
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==About this Structure==
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1QUU is a [[Single protein]] 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=1QUU OCA].
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==Reference==
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Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments., Djinovic-Carugo K, Young P, Gautel M, Saraste M, Cell. 1999 Aug 20;98(4):537-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10481917 10481917]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Djinovic-Carugo, K.]]
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[[Category: Djinovic-Carugo K]]
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[[Category: Gautel, M.]]
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[[Category: Gautel M]]
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[[Category: Saraste, M.]]
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[[Category: Saraste M]]
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[[Category: Young, P.]]
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[[Category: Young P]]
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[[Category: triple-helix coiled coil]]
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[[Category: Z-disk]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:19:22 2008''
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Current revision

CRYSTAL STRUCTURE OF TWO CENTRAL SPECTRIN-LIKE REPEATS FROM ALPHA-ACTININ

PDB ID 1quu

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