3ekj: Difference between revisions

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 ==Calcium-free GCaMP2 (calcium binding deficient mutant)==
-<StructureSection load='3ekj' size='340' side='right' caption='[[3ekj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
+<StructureSection load='3ekj' size='340' side='right'caption='[[3ekj]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ekj]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EKJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3EKJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ekj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria], [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3EKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EKJ FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ek4|3ek4]], [[3ek7|3ek7]], [[3ek8|3ek8]], [[3ekh|3ekh]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></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=3ekj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ekj OCA], [http://pdbe.org/3ekj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ekj RCSB], [http://www.ebi.ac.uk/pdbsum/3ekj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ekj ProSAT]</span></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=3ekj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ekj OCA], [https://pdbe.org/3ekj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ekj RCSB], [https://www.ebi.ac.uk/pdbsum/3ekj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ekj ProSAT]</span></td></tr>
 </table>
+== Function ==
+[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.[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 21: @@
 ==See Also==
-*[[Calmodulin|Calmodulin]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
-*[[Green Fluorescent Protein|Green Fluorescent Protein]]
+*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Akerboom, J]]
+[[Category: Aequorea victoria]]
-[[Category: Looger, L L]]
+[[Category: Large Structures]]
-[[Category: Rivera, J D.Velez]]
+[[Category: Rattus norvegicus]]
-[[Category: Schreiter, E R]]
+[[Category: Synthetic construct]]
-[[Category: Apo gcamp2]]
+[[Category: Akerboom J]]
-[[Category: Calcium-free]]
+[[Category: Looger LL]]
-[[Category: Calmodulin]]
+[[Category: Schreiter ER]]
-[[Category: Cpgfp]]
+[[Category: Velez Rivera JD]]
-[[Category: Fluorescent protein]]
-[[Category: Gcamp2]]
-[[Category: Geci]]
-[[Category: M13 peptide]]
-[[Category: Signaling protein]]