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1cdm

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(New page: 200px<br /><applet load="1cdm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cdm, resolution 2.0&Aring;" /> '''MODULATION OF CALMODU...)
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[[Image:1cdm.gif|left|200px]]<br /><applet load="1cdm" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cdm, resolution 2.0&Aring;" />
 
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'''MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES'''<br />
 
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==Overview==
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==MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES==
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Calmodulin is the primary calcium-dependent signal transducer and, regulator of a wide variety of essential cellular functions. The structure, of calcium-calmodulin bound to the peptide corresponding to the, calmodulin-binding domain of brain calmodulin-dependent protein kinase II, alpha was determined to 2 angstrom resolution. A comparison to two other, calcium-calmodulin structures reveals how the central helix unwinds in, order to position the two domains optimally in the recognition of, different target enzymes and clarifies the role of calcium in maintaining, recognition-competent domain structures.
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<StructureSection load='1cdm' size='340' side='right'caption='[[1cdm]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cdm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CDM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cdm OCA], [https://pdbe.org/1cdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cdm RCSB], [https://www.ebi.ac.uk/pdbsum/1cdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cdm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cd/1cdm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1cdm ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1CDM is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CDM OCA].
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Modulation of calmodulin plasticity in molecular recognition on the basis of x-ray structures., Meador WE, Means AR, Quiocho FA, Science. 1993 Dec 10;262(5140):1718-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8259515 8259515]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Meador, W.E.]]
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[[Category: Meador WE]]
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[[Category: Quiocho, F.A.]]
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[[Category: Quiocho FA]]
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[[Category: CA]]
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[[Category: calcium-binding protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:22:11 2007''
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Current revision

MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES

PDB ID 1cdm

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