1qx5

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[[Image:1qx5.gif|left|200px]]
 
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{{Structure
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==Crystal structure of apoCalmodulin==
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|PDB= 1qx5 |SIZE=350|CAPTION= <scene name='initialview01'>1qx5</scene>, resolution 2.54&Aring;
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<StructureSection load='1qx5' size='340' side='right'caption='[[1qx5]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1qx5]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QX5 FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.54&#8491;</td></tr>
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|GENE= CALM1, CAM1, CALM, CAM, CALM2, CAM2, CAMB, CALM3, CAM3, CAMC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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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=1qx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx5 OCA], [https://pdbe.org/1qx5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qx5 RCSB], [https://www.ebi.ac.uk/pdbsum/1qx5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qx5 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1cfc|1CFC]], [[1cfd|1CFD]], [[1cll|1CLL]], [[1g4y|1G4Y]], [[1qx7|1QX7]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qx5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qx5 OCA], [http://www.ebi.ac.uk/pdbsum/1qx5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qx5 RCSB]</span>
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[https://www.uniprot.org/uniprot/CALM1_RAT CALM1_RAT] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2.[UniProtKB:P62158]
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}}
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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/qx/1qx5_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=1qx5 ConSurf].
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<div style="clear:both"></div>
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'''Crystal structure of apoCalmodulin'''
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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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Small conductance Ca2+-activated K+ channels (SK channels) are composed of the pore-forming alpha subunit and calmodulin (CaM). CaM binds to a region of the alpha subunit called the CaM binding domain (CaMBD), located intracellular and immediately C-terminal to the inner helix gate, in either the presence or absence of Ca2+. SK gating occurs when Ca2+ binds the N lobe of CaM thereby transmitting the signal to the attached inner helix gate to open. Here we present crystal structures of apoCaM and apoCaM/SK2 CaMBD complex. Several apoCaM crystal forms with multiple (12) packing environments reveal the same EF hand domain-swapped dimer providing potentially new insight into CaM regulation. The apoCaM/SK2 CaMBD structure, combined with our Ca2+/CaM/CaMBD structure suggests that Ca2+ binding induces folding and dimerization of the CaMBD, which causes large CaMBD-CaM C lobe conformational changes, including a &gt;90 degrees rotation of the region of the CaMBD directly connected to the gate.
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[[Category: Large Structures]]
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==About this Structure==
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1QX5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QX5 OCA].
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==Reference==
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Crystal structures of apocalmodulin and an apocalmodulin/SK potassium channel gating domain complex., Schumacher MA, Crum M, Miller MC, Structure. 2004 May;12(5):849-60. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15130477 15130477]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Crum M]]
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[[Category: Crum, M.]]
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[[Category: Miller MC]]
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[[Category: Miller, M C.]]
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[[Category: Schumacher MA]]
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[[Category: Schumacher, M A.]]
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[[Category: apocalmodulin]]
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[[Category: calcium binding protein]]
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[[Category: dimer,ef hand]]
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[[Category: domain swap]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:15 2008''
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Current revision

Crystal structure of apoCalmodulin

PDB ID 1qx5

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