1cmf

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{{Seed}}
 
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[[Image:1cmf.png|left|200px]]
 
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==NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN==
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The line below this paragraph, containing "STRUCTURE_1cmf", creates the "Structure Box" on the page.
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<StructureSection load='1cmf' size='340' side='right'caption='[[1cmf]]' 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'>[[1cmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CMF 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=1cmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmf OCA], [https://pdbe.org/1cmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmf RCSB], [https://www.ebi.ac.uk/pdbsum/1cmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmf ProSAT]</span></td></tr>
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{{STRUCTURE_1cmf| PDB=1cmf | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM_BOVIN CALM_BOVIN] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity).
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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/cm/1cmf_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=1cmf 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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We have determined the solution structures of the apo and (Ca2+)2 forms of the carboxy-terminal domain of calmodulin using multidimensional heteronuclear nuclear magnetic resonance spectroscopy. The results show that both forms adopt well-defined structures with essentially equal secondary structure. A comparison of the structures of the two forms shows that Ca2+ binding causes major rearrangements of the secondary structure elements with changes in inter-residue distances of up to 15 A and exposure of the hydrophobic interior of the four-helix bundle. Comparisons with previously determined high-resolution X-ray structures and models of calmodulin indicate that this domain is structurally autonomous.
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===NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN===
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Calcium-induced structural changes and domain autonomy in calmodulin.,Finn BE, Evenas J, Drakenberg T, Waltho JP, Thulin E, Forsen S Nat Struct Biol. 1995 Sep;2(9):777-83. PMID:7552749<ref>PMID:7552749</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_7552749}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1cmf" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 7552749 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_7552749}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1CMF is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMF OCA].
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==Reference==
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<ref group="xtra">PMID:7552749</ref><references group="xtra"/>
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Drakenberg, T.]]
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[[Category: Large Structures]]
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[[Category: Evenas, J.]]
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[[Category: Drakenberg T]]
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[[Category: Finn, B E.]]
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[[Category: Evenas J]]
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[[Category: Forsen, S.]]
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[[Category: Finn BE]]
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[[Category: Thulin, E.]]
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[[Category: Forsen S]]
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[[Category: Waltho, J P.]]
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[[Category: Thulin E]]
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[[Category: Calcium-binding protein]]
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[[Category: Waltho JP]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:34:43 2009''
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Current revision

NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN

PDB ID 1cmf

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