1cmf: Difference between revisions
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<StructureSection load='1cmf' size='340' side='right' caption='[[1cmf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1cmf' size='340' side='right' caption='[[1cmf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cmf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1cmf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CMF FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cmf RCSB], [http://www.ebi.ac.uk/pdbsum/1cmf PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmf OCA], [http://pdbe.org/1cmf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cmf RCSB], [http://www.ebi.ac.uk/pdbsum/1cmf PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1cmf" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bovin]] | ||
[[Category: Drakenberg, T]] | [[Category: Drakenberg, T]] | ||
[[Category: Evenas, J]] | [[Category: Evenas, J]] | ||
Revision as of 09:18, 10 September 2015
NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAINNMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN
Structural highlights
Function[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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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