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New page: left|200px<br /><applet load="1cmf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cmf" /> '''NMR SOLUTION STRUCTURE OF APO CALMODULIN CAR... |
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== | ==NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN== | ||
We have determined the solution structures of the apo and (Ca2+)2 forms of | <StructureSection load='1cmf' size='340' side='right'caption='[[1cmf]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1cmf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1CMF 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=1cmf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cmf OCA], [https://pdbe.org/1cmf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cmf RCSB], [https://www.ebi.ac.uk/pdbsum/1cmf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cmf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/CALM_BOVIN 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 == | |||
[[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/cm/1cmf_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=1cmf ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We 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<ref>PMID:7552749</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cmf" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Drakenberg | [[Category: Drakenberg T]] | ||
[[Category: Evenas | [[Category: Evenas J]] | ||
[[Category: Finn | [[Category: Finn BE]] | ||
[[Category: Forsen | [[Category: Forsen S]] | ||
[[Category: Thulin | [[Category: Thulin E]] | ||
[[Category: Waltho | [[Category: Waltho JP]] | ||
Latest revision as of 11:21, 22 May 2024
NMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAINNMR SOLUTION STRUCTURE OF APO CALMODULIN CARBOXY-TERMINAL DOMAIN
Structural highlights
FunctionCALM_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. References |
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