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1cfc

From Proteopedia

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[[Image:1cfc.png|left|200px]]
 
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==CALCIUM-FREE CALMODULIN==
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The line below this paragraph, containing "STRUCTURE_1cfc", creates the "Structure Box" on the page.
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<StructureSection load='1cfc' size='340' side='right'caption='[[1cfc]]' 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'>[[1cfc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFC 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=1cfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfc OCA], [https://pdbe.org/1cfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfc RCSB], [https://www.ebi.ac.uk/pdbsum/1cfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfc ProSAT]</span></td></tr>
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{{STRUCTURE_1cfc| PDB=1cfc | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] 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.
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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/cf/1cfc_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=1cfc 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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The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J-couplings. In analogy with the Ca(2+)-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca2+, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel beta-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca(2+)-free N-terminal domain of troponin C.
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===CALCIUM-FREE CALMODULIN===
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Solution structure of calcium-free calmodulin.,Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A Nat Struct Biol. 1995 Sep;2(9):768-76. PMID:7552748<ref>PMID:7552748</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_7552748}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1cfc" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 7552748 is the PubMed ID number.
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-->
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{{ABSTRACT_PUBMED_7552748}}
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==About this Structure==
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[[1cfc]] is a 1 chain structure of [[Calmodulin]] with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFC OCA].
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==See Also==
==See Also==
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*[[Calmodulin]]
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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*[[Hydrogen in macromolecular models|Hydrogen in macromolecular models]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:7552748</ref><references group="xtra"/>
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Bax, A.]]
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[[Category: Bax A]]
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[[Category: Grzesiek, S.]]
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[[Category: Grzesiek S]]
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[[Category: Klee, C B.]]
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[[Category: Klee CB]]
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[[Category: Kuboniwa, H.]]
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[[Category: Kuboniwa H]]
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[[Category: Ren, H.]]
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[[Category: Ren H]]
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[[Category: Tjandra, N.]]
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[[Category: Tjandra N]]
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[[Category: Calcium-binding protein]]
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Current revision

CALCIUM-FREE CALMODULIN

PDB ID 1cfc

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