1h67

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{{Seed}}
 
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[[Image:1h67.png|left|200px]]
 
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==NMR Structure of the CH Domain of Calponin==
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The line below this paragraph, containing "STRUCTURE_1h67", creates the "Structure Box" on the page.
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<StructureSection load='1h67' size='340' side='right'caption='[[1h67]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1h67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H67 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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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=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [https://pdbe.org/1h67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB], [https://www.ebi.ac.uk/pdbsum/1h67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h67 ProSAT]</span></td></tr>
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{{STRUCTURE_1h67| PDB=1h67 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CNN1_CHICK CNN1_CHICK] Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity.
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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/h6/1h67_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=1h67 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Calponin is involved in the regulation of contractility and organization of the actin cytoskeleton in smooth muscle cells. It is the archetypal member of the calponin homology (CH) domain family of actin binding proteins that includes cytoskeletal linkers such as alpha-actinin, spectrin, and dystrophin, and regulatory proteins including VAV, IQGAP, and calponin. We have determined the first structure of a CH domain from a single CH domain-containing protein, that of calponin, and have fitted the NMR-derived coordinates to the 3D-helical reconstruction of the F-actin:calponin complex using cryo-electron microscopy. The tertiary fold of this single CH domain is typical of, yet significantly different from, those of the CH domains that occur in tandem pairs to form high-affinity ABDs in other proteins. We thus provide a structural insight into the mode of interaction between F-actin and CH domain-containing proteins.
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===NMR STRUCTURE OF THE CH DOMAIN OF CALPONIN===
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Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin.,Bramham J, Hodgkinson JL, Smith BO, Uhrin D, Barlow PN, Winder SJ Structure. 2002 Feb;10(2):249-58. PMID:11839310<ref>PMID:11839310</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11839310}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1h67" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11839310 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11839310}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1H67 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H67 OCA].
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==Reference==
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Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin., Bramham J, Hodgkinson JL, Smith BO, Uhrin D, Barlow PN, Winder SJ, Structure. 2002 Feb;10(2):249-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11839310 11839310]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Barlow, P N.]]
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[[Category: Barlow PN]]
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[[Category: Bramham, J.]]
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[[Category: Bramham J]]
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[[Category: Smith, B O.]]
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[[Category: Smith BO]]
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[[Category: Uhrin, D.]]
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[[Category: Uhrin D]]
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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: Nmr]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:41:28 2008''
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Current revision

NMR Structure of the CH Domain of Calponin

PDB ID 1h67

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