1cfd: Difference between revisions
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== | ==CALCIUM-FREE CALMODULIN== | ||
<StructureSection load='1cfd' size='340' side='right'caption='[[1cfd]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1cfd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The August 2003 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Calmodulin'' by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2003_8 10.2210/rcsb_pdb/mom_2003_8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfd OCA], [https://pdbe.org/1cfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfd RCSB], [https://www.ebi.ac.uk/pdbsum/1cfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cf/1cfd_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1cfd ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | 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. | ||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cfd" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Calmodulin 3D structures|Calmodulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Calmodulin]] | [[Category: Calmodulin]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | |||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Bax | [[Category: Bax A]] | ||
[[Category: Grzesiek | [[Category: Grzesiek S]] | ||
[[Category: Klee | [[Category: Klee CB]] | ||
[[Category: Kuboniwa | [[Category: Kuboniwa H]] | ||
[[Category: Ren | [[Category: Ren H]] | ||
[[Category: Tjandra | [[Category: Tjandra N]] | ||
Latest revision as of 08:21, 22 May 2024
CALCIUM-FREE CALMODULIN
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