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1cfc

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[[Image:1cfc.gif|left|200px]]
 
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{{Structure
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==CALCIUM-FREE CALMODULIN==
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|PDB= 1cfc |SIZE=350|CAPTION= <scene name='initialview01'>1cfc</scene>
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<StructureSection load='1cfc' size='340' side='right'caption='[[1cfc]]' 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'>[[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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|ACTIVITY=
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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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|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=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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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1cfd|1CFD]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfc OCA], [http://www.ebi.ac.uk/pdbsum/1cfc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cfc RCSB]</span>
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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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}}
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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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<div class="pdbe-citations 1cfc" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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*[[Hydrogen in macromolecular models|Hydrogen in macromolecular models]]
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==About this Structure==
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== References ==
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1CFC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFC OCA].
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<references/>
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__TOC__
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==Reference==
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</StructureSection>
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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:[http://www.ncbi.nlm.nih.gov/pubmed/7552748 7552748]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:20:33 2008''
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Current revision

CALCIUM-FREE CALMODULIN

PDB ID 1cfc

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