1cfc
From Proteopedia
(Difference between revisions)
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| - | + | ==CALCIUM-FREE CALMODULIN== | |
| - | === | + | <StructureSection load='1cfc' size='340' side='right' caption='[[1cfc]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''> |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[1cfc]] is a 1 chain structure 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CFC FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cfd|1cfd]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1cfc RCSB], [http://www.ebi.ac.uk/pdbsum/1cfc PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == 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/1cfc_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/chain_selection.php?pdb_ID=2ata 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. | ||
| - | + | 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> | ||
==See Also== | ==See Also== | ||
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*[[NMR Ensembles of Models|NMR Ensembles of Models]] | *[[NMR Ensembles of Models|NMR Ensembles of Models]] | ||
*[[Structural alignment tools|Structural alignment tools]] | *[[Structural alignment tools|Structural alignment tools]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Bax, A.]] | [[Category: Bax, A.]] | ||
Revision as of 13:57, 29 September 2014
CALCIUM-FREE CALMODULIN
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