Calmodulin

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[[Image:1prw.png|left|200px|thumb|Crystal structure of bovine brain Ca++ calmodulin in a compact form, [[1prw]]]]
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<StructureSection load='1cll' size='350' side='right' scene='39/398280/Cv/3' caption='Human calmodulin complex with ethanol and Ca+2 ions (green) (PDB code [[1cll]])'>
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{{STRUCTURE_1prw| PDB=1prw | SIZE=300| SCENE= |right|CAPTION=Calmodulin, [[1prw]] }}
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__TOC__
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==Function==
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Under contstruction...
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[[Calmodulin]] (CaM) – calcium modulated protein – regulates various protein targets. It is used by various proteins as calcium sensor and signal transducer by binding to their calcium binding domain (CBD). It undergoes conformational change upon binding Ca++ via its 4 [[EF hand]] motives and can undergo post-translational modification. <scene name='39/398280/Cv/4'>Click here to see EF hand</scene> of Human calmodulin (PDB code [[1cll]]). <ref>PMID:1474585</ref> More details on apo-CaM [[Calcium-free Calmodulin]] and [[Calmodulin JMU]].
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[[Calmodulin]] (CaM) – calcium modulated protein – regulates various protein targets. It is used by various proteins as calcium sensor and signal transducer by binding to their calcium binding domain (CBD). It undergoes conformational change upon binding Ca++ via its 4 EF hand motives and can undergo post-translational modification.
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The images at the left and at the right correspond to one representative calmodulin, ''i.e.'' crystal structure of bovine brain Ca++ calmodulin in a compact form ([[1prw]]).
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{{TOC limit|limit=2}}
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{{Clear}}
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== [[Maximum Occurrence]] of Calmodulin Conformations ==
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<applet load='1cll' size='350' color='white' frame='true' align='right' caption='Calmodulin' scene='Calmodulin/Inicio/1' />
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[[Maximum Occurrence]], a method for making rigorous numerical assessments about the maximum percent of time that a conformer of a flexible macromolecule can exist and still be compatible with the experimental data, was used to probe the conformational disorder of Calmodulin<ref>doi:10.1021/ja1063923</ref>.<br />
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[[Image:Movie_MOforproteopedia.gif|thumb|center|400px|Figure 3: Orientation tensor representation for 400 conformational states of Calmodulin, color coded according to their MO values (from less than 5% in blue to more than 30% in red).To better explain their meaning, 10 randomly chosen models are shown as cartoons and then replaced by the three axes of their color-coded orientation tensors.]] <br />
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It was shown that the open ([[1cll]]) and closed ([[1prw]]) conformers can have MO of only 15% and 5% respectively.
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== Calmodulin in Motion ==
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The buttons below allow you to explore morphs <ref>The [[Jmol/Storymorph|Storymorph Jmol scripts]] creates the interpolated coordinates of the morph on the fly.</ref> between structures [[1prw]] and [[1cll]].
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[http://www.molmovdb.org/cgi-bin/morph.cgi?ID=b097743-28520 Conformational change of Calmodulin]
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<jmol>
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<jmolButton>
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<script>
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script "/wiki/images/a/a2/Storymorph.spt";
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load files "=1prw" "=1cll";
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delete water;
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delete protein and not backbone;
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select all;cartoon only;cartoon off;
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select 4-147;cartoon on;
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model 1;
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center visible;color group;
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compare {2.1} {1.1} SUBSET{*.CA} ATOMS{4-138}{4-138} ROTATE TRANSLATE;
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</script>
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<text>Prepare Animation</text>
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</jmolButton>
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</jmol><jmol>
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<jmolButton>
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<script>
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model 2;
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display 4-147;
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backbone only;
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backbone 0.5
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structures = [{1.1}, {2.1}];
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my_recipe = [
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[{79-147},{79-147}, {(79-138) and alpha}],
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[{4-78}, {79}, {(8-78) and alpha}],
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];
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morph(20, structures, my_recipe);
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</script>
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<text>Open</text>
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</jmolButton>
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</jmol><jmol>
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<jmolButton>
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<script>
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model 1
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display 4-147;
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backbone only;
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backbone 0.5
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structures = [{2.1}, {1.1}];
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my_recipe = [
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[{79-147},{79-147}, {(79-138) and alpha}],
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[{4-78}, {79}, {(8-78) and alpha}],
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];
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morph(20, structures, my_recipe);
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</script>
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<text>Close</text>
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</jmolButton>
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</jmol>
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[http://www.proteopedia.org/wiki/index.php/Calmodulin_in_motion Calmodulin in Motion]
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The following morph is between [[1prw]] and [[1cll]] after superposition of residues 79-138. This shows the subtle conformational changes in that domain more clearly.
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<jmol>
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<jmolButton>
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<script>
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script "/wiki/images/a/a2/Storymorph.spt";
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load files "=1prw" "=1cll";
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delete water;
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delete protein and not backbone;
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select all;cartoon only;cartoon off;
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select 4-147;cartoon on;
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model 1;
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center visible;color group;
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compare {2.1} {1.1} SUBSET{*.CA} ATOMS{79-138}{79-138} ROTATE TRANSLATE;
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</script>
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<text>Prepare Animation</text>
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</jmolButton>
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</jmol><jmol>
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<jmolButton>
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<script>
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model 2;
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display 4-147;
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backbone only;
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backbone 0.5
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structures = [{1.1}, {2.1}];
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my_recipe = [
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[{79-147},{79-147}, {(79-138) and alpha}],
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[{4-78}, {79}, {(8-78) and alpha}],
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];
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morph(20, structures, my_recipe);
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</script>
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<text>Open</text>
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</jmolButton>
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</jmol><jmol>
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<jmolButton>
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<script>
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model 1
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display 4-147;
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backbone only;
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backbone 0.5
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structures = [{2.1}, {1.1}];
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my_recipe = [
 +
[{79-147},{79-147}, {(79-138) and alpha}],
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[{4-78}, {79}, {(8-78) and alpha}],
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];
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morph(20, structures, my_recipe);
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</script>
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<text>Close</text>
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</jmolButton>
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</jmol>
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The following morph is between [[1prw]] and [[1cll]] after superposition of residues 8-78. This shows the subtle conformational changes in that domain more clearly.
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<jmol>
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<jmolButton>
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<script>
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script "/wiki/images/a/a2/Storymorph.spt";
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load files "=1prw" "=1cll";
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delete water;
 +
delete protein and not backbone;
 +
select all;cartoon only;cartoon off;
 +
select 4-147;cartoon on;
 +
model 1;
 +
center visible;color group;
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compare {2.1} {1.1} SUBSET{*.CA} ATOMS{8-78}{8-78} ROTATE TRANSLATE;
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</script>
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<text>Prepare Animation</text>
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</jmolButton>
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</jmol><jmol>
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<jmolButton>
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<script>
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model 2;
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display 4-147;
 +
backbone only;
 +
backbone 0.5
 +
structures = [{1.1}, {2.1}];
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my_recipe = [
 +
[{4-78}, {4-78}, {(8-78) and alpha}],
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[{79-147},{78}, {(79-138) and alpha}],
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];
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morph(20, structures, my_recipe);
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</script>
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<text>Open</text>
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</jmolButton>
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</jmol><jmol>
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<jmolButton>
 +
<script>
 +
model 1
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display 4-147;
 +
backbone only;
 +
backbone 0.5
 +
structures = [{2.1}, {1.1}];
 +
my_recipe = [
 +
[{4-78}, {4-78}, {(8-78) and alpha}],
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[{79-147},{78}, {(79-138) and alpha}],
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];
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morph(20, structures, my_recipe);
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</script>
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<text>Close</text>
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</jmolButton>
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</jmol>
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<scene name='Calmodulin/Inicio/1'>Unbound</scene>,
 
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<scene name='Calmodulin/Bound/3'>Bound</scene>
 
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== 3D Structures of Calmodulin ==
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[[Calmodulin 3D structures]]
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</StructureSection>
==See Also==
==See Also==
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* [http://en.wikipedia.org/wiki/Calmodulin Calmodulin at Wikipedia]
* [http://en.wikipedia.org/wiki/Calmodulin Calmodulin at Wikipedia]
* [http://www.pdb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb44_1.html Molecule of the Month (08/2003) at RCSB PDB]
* [http://www.pdb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb44_1.html Molecule of the Month (08/2003) at RCSB PDB]
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*{{Proteopedia|2fot}} page for Calmodulin crystal complex between calmodulin and alpha11-[[spectrin]]
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== Bibliography ==
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<references/>
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[[Category:Topic Page]]

Current revision

Human calmodulin complex with ethanol and Ca+2 ions (green) (PDB code 1cll)

Drag the structure with the mouse to rotate

See Also

Bibliography

  1. ↑ Chattopadhyaya R, Meador WE, Means AR, Quiocho FA. Calmodulin structure refined at 1.7 A resolution. J Mol Biol. 1992 Dec 20;228(4):1177-92. PMID:1474585
  2. ↑ Bertini I, Giachetti A, Luchinat C, Parigi G, Petoukhov MV, Pierattelli R, Ravera E, Svergun DI. Conformational Space of Flexible Biological Macromolecules from Average Data. J Am Chem Soc. 2010 Sep 7. PMID:20822180 doi:10.1021/ja1063923
  3. ↑ The Storymorph Jmol scripts creates the interpolated coordinates of the morph on the fly.
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