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1qag

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(New page: 200px<br /> <applet load="1qag" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qag, resolution 3.00&Aring;" /> '''Actin binding regio...)
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[[Image:1qag.gif|left|200px]]<br />
 
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<applet load="1qag" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qag, resolution 3.00&Aring;" />
 
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'''Actin binding region of the dystrophin homologue utrophin'''<br />
 
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==Overview==
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==Actin binding region of the dystrophin homologue utrophin==
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BACKGROUND: Utrophin is a large multidomain protein that belongs to a, superfamily of actin-binding proteins, which includes dystrophin, alpha-actinin, beta-spectrin, fimbrin, filamin and plectin. All the, members of this family contain a common actin-binding region at their N, termini and perform a wide variety of roles associated with the actin, cytoskeleton. Utrophin is the autosomal homologue of dystrophin, the, protein defective in the X-linked Duchenne and Becker muscular, dystrophies, and upregulation of utrophin has been suggested as a, potential therapy for muscular dystrophy patients. RESULTS: The structure, of the actin-binding region of utrophin, consisting of two, calponin-homology (CH) domains, has been solved at 3.0 A resolution. It is, composed of an antiparallel dimer with each of the monomers being present, in an extended dumbell shape and the two CH domains being separated by a, long central helix. This extended conformation is in sharp contrast to the, compact monomer structure of the N-terminal actin-binding region of, fimbrin. CONCLUSIONS: The crystal structure of the actin-binding region of, utrophin suggests that these actin-binding domains may be more flexible, than was previously thought and that this flexibility may allow domain, reorganisation and play a role in the actin-binding mechanism. Thus, utrophin could possibly bind to actin in an extended conformation so that, the sites previously identified as being important for actin binding may, be directly involved in this interaction.
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<StructureSection load='1qag' size='340' side='right'caption='[[1qag]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1qag]] 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=1QAG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QAG FirstGlance]. <br>
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1QAG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QAG OCA].
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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]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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==Reference==
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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=1qag FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qag OCA], [https://pdbe.org/1qag PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qag RCSB], [https://www.ebi.ac.uk/pdbsum/1qag PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qag ProSAT]</span></td></tr>
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Crystal structure of the actin-binding region of utrophin reveals a head-to-tail dimer., Keep NH, Winder SJ, Moores CA, Walke S, Norwood FL, Kendrick-Jones J, Structure. 1999 Dec 15;7(12):1539-46. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10647184 10647184]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/UTRN_HUMAN UTRN_HUMAN] May play a role in anchoring the cytoskeleton to the plasma membrane.
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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/qa/1qag_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=1qag ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[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: Keep, N.H.]]
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[[Category: Keep NH]]
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[[Category: Kendrick-Jones, J.]]
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[[Category: Kendrick-Jones J]]
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[[Category: Moores, C.A.]]
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[[Category: Moores CA]]
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[[Category: Norwood, F.L.M.]]
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[[Category: Norwood FLM]]
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[[Category: Walke, S.]]
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[[Category: Walke S]]
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[[Category: Winder, S.J.]]
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[[Category: Winder SJ]]
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[[Category: actin binding]]
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[[Category: calponin homology domain]]
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[[Category: domain swapping]]
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[[Category: dystrophin]]
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[[Category: utrophin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:51:56 2007''
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Current revision

Actin binding region of the dystrophin homologue utrophin

PDB ID 1qag

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