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| | <StructureSection load='4oy4' size='340' side='right'caption='[[4oy4]], [[Resolution|resolution]] 2.03Å' scene=''> | | <StructureSection load='4oy4' size='340' side='right'caption='[[4oy4]], [[Resolution|resolution]] 2.03Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4oy4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OY4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OY4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4oy4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus], [https://en.wikipedia.org/wiki/Lobophyllia_hemprichii Lobophyllia hemprichii] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OY4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OY4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CR8:2-[1-AMINO-2-(1H-IMIDAZOL-5-YL)ETHYL]-1-(CARBOXYMETHYL)-4-[(4-OXOCYCLOHEXA-2,5-DIEN-1-YLIDENE)METHYL]-1H-IMIDAZOL-5-OLATE'>CR8</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CR8:2-[1-AMINO-2-(1H-IMIDAZOL-5-YL)ETHYL]-1-(CARBOXYMETHYL)-4-[(4-OXOCYCLOHEXA-2,5-DIEN-1-YLIDENE)METHYL]-1H-IMIDAZOL-5-OLATE'>CR8</scene></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=4oy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oy4 OCA], [https://pdbe.org/4oy4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oy4 RCSB], [https://www.ebi.ac.uk/pdbsum/4oy4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oy4 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Calm1, Calm, Cam, Cam1, Calm2, Cam2, Camb, Calm3, Cam3, Camc ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9031 CHICK])</td></tr> | + | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oy4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oy4 OCA], [http://pdbe.org/4oy4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oy4 RCSB], [http://www.ebi.ac.uk/pdbsum/4oy4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oy4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5S6Z9_LOBHE Q5S6Z9_LOBHE] [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][https://www.uniprot.org/uniprot/MYLK_CHICK MYLK_CHICK] Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fosque, B F]] | + | [[Category: Lobophyllia hemprichii]] |
| - | [[Category: Schreiter, E R]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Calcium]] | + | [[Category: Fosque BF]] |
| - | [[Category: Calcium binding]] | + | [[Category: Schreiter ER]] |
| - | [[Category: Engineered protein]]
| + | |
| - | [[Category: Fluorescent]]
| + | |
| - | [[Category: Fluorescent protein]]
| + | |
| - | [[Category: Integrator]]
| + | |
| - | [[Category: Photoconversion]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q5S6Z9_LOBHE 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]MYLK_CHICK Phosphorylates a specific serine in the N-terminus of a myosin light chain, which leads to the formation of calmodulin/MLCK signal transduction complexes which allow selective transduction of calcium signals.
Publication Abstract from PubMed
The identification of active neurons and circuits in vivo is a fundamental challenge in understanding the neural basis of behavior. Genetically encoded calcium (Ca(2+)) indicators (GECIs) enable quantitative monitoring of cellular-resolution activity during behavior. However, such indicators require online monitoring within a limited field of view. Alternatively, post hoc staining of immediate early genes (IEGs) indicates highly active cells within the entire brain, albeit with poor temporal resolution. We designed a fluorescent sensor, CaMPARI, that combines the genetic targetability and quantitative link to neural activity of GECIs with the permanent, large-scale labeling of IEGs, allowing a temporally precise "activity snapshot" of a large tissue volume. CaMPARI undergoes efficient and irreversible green-to-red conversion only when elevated intracellular Ca(2+) and experimenter-controlled illumination coincide. We demonstrate the utility of CaMPARI in freely moving larvae of zebrafish and flies, and in head-fixed mice and adult flies.
Neural circuits. Labeling of active neural circuits in vivo with designed calcium integrators.,Fosque BF, Sun Y, Dana H, Yang CT, Ohyama T, Tadross MR, Patel R, Zlatic M, Kim DS, Ahrens MB, Jayaraman V, Looger LL, Schreiter ER Science. 2015 Feb 13;347(6223):755-60. doi: 10.1126/science.1260922. PMID:25678659[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fosque BF, Sun Y, Dana H, Yang CT, Ohyama T, Tadross MR, Patel R, Zlatic M, Kim DS, Ahrens MB, Jayaraman V, Looger LL, Schreiter ER. Neural circuits. Labeling of active neural circuits in vivo with designed calcium integrators. Science. 2015 Feb 13;347(6223):755-60. doi: 10.1126/science.1260922. PMID:25678659 doi:http://dx.doi.org/10.1126/science.1260922
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