2bcx

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[[Image:2bcx.jpg|left|200px]]
 
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==Crystal structure of calmodulin in complex with a ryanodine receptor peptide==
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The line below this paragraph, containing "STRUCTURE_2bcx", creates the "Structure Box" on the page.
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<StructureSection load='2bcx' size='340' side='right'caption='[[2bcx]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2bcx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BCX FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_2bcx| PDB=2bcx | SCENE= }}
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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=2bcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bcx OCA], [https://pdbe.org/2bcx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bcx RCSB], [https://www.ebi.ac.uk/pdbsum/2bcx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bcx ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK] 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.
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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/bc/2bcx_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=2bcx ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of calmodulin in complex with a ryanodine receptor peptide'''
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==See Also==
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Calmodulin regulates ryanodine receptor-mediated Ca(2+) release through a conserved binding site. The crystal structure of Ca(2+)-calmodulin bound to this conserved site reveals that calmodulin recognizes two hydrophobic anchor residues at a novel "1-17" spacing that brings the calmodulin lobes close together but prevents them from contacting one another. NMR residual dipolar couplings demonstrate that the detailed structure of each lobe is preserved in solution but also show that the lobes experience domain motions within the complex. FRET measurements confirm the close approach of the lobes in binding the 1-17 target and show that calmodulin binds with one lobe to a peptide lacking the second anchor. We suggest that calmodulin regulates the Ca(2+) channel by switching between the contiguous binding mode seen in our crystal structure and a state where one lobe of calmodulin contacts the conserved binding site while the other interacts with a noncontiguous site on the channel.
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==About this Structure==
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2BCX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCX OCA].
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==Reference==
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Complex of calmodulin with a ryanodine receptor target reveals a novel, flexible binding mode., Maximciuc AA, Putkey JA, Shamoo Y, Mackenzie KR, Structure. 2006 Oct;14(10):1547-56. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17027503 17027503]
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: MacKenzie, K R.]]
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[[Category: Oryctolagus cuniculus]]
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[[Category: Maximciuc, A A.]]
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[[Category: MacKenzie KR]]
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[[Category: Shamoo, Y.]]
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[[Category: Maximciuc AA]]
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[[Category: Ef-hand]]
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[[Category: Shamoo Y]]
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[[Category: Type-2 turn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 20:07:28 2008''
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Current revision

Crystal structure of calmodulin in complex with a ryanodine receptor peptide

PDB ID 2bcx

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