2kdu: Difference between revisions

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 ==Structural basis of the Munc13-1/Ca2+-Calmodulin interaction: A novel 1-26 calmodulin binding motif with a bipartite binding mode==
-<StructureSection load='2kdu' size='340' side='right' caption='[[2kdu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2kdu' size='340' side='right'caption='[[2kdu]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kdu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/African_clawed_frog African clawed frog]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KDU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kdu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KDU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">calm1, calm2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8355 African clawed frog])</td></tr>
+<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>
-<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=2kdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdu OCA], [http://pdbe.org/2kdu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kdu RCSB], [http://www.ebi.ac.uk/pdbsum/2kdu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdu 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=2kdu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdu OCA], [https://pdbe.org/2kdu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kdu RCSB], [https://www.ebi.ac.uk/pdbsum/2kdu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] 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. [[http://www.uniprot.org/uniprot/UN13A_RAT UN13A_RAT]] Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Also involved in secretory granule priming in insulin secretion.<ref>PMID:9697857</ref> <ref>PMID:11343654</ref> <ref>PMID:11792326</ref>
+[https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] 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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Calmodulin|Calmodulin]]
+*[[Calmodulin 3D structures|Calmodulin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: African clawed frog]]
+[[Category: Large Structures]]
-[[Category: Becker, S]]
+[[Category: Rattus norvegicus]]
-[[Category: Brose, N]]
+[[Category: Xenopus laevis]]
-[[Category: Carlomagno, T]]
+[[Category: Becker S]]
-[[Category: Coudevylle, N]]
+[[Category: Brose N]]
-[[Category: Dimova, K]]
+[[Category: Carlomagno T]]
-[[Category: Griesinger, C]]
+[[Category: Coudevylle N]]
-[[Category: Jahn, O]]
+[[Category: Dimova K]]
-[[Category: Junge, H]]
+[[Category: Griesinger C]]
-[[Category: Maestre-Martinez, M]]
+[[Category: Jahn O]]
-[[Category: Rodriguez-Castaneda, F A]]
+[[Category: Junge H]]
-[[Category: Acetylation]]
+[[Category: Maestre-Martinez M]]
-[[Category: Alternative splicing]]
+[[Category: Rodriguez-Castaneda FA]]
-[[Category: Calcium]]
-[[Category: Calmodulin]]
-[[Category: Cell junction]]
-[[Category: Cell membrane]]
-[[Category: Coiled coil]]
-[[Category: Cytoplasm]]
-[[Category: Exocytosis]]
-[[Category: Membrane]]
-[[Category: Metal binding protein-exocytosis complex]]
-[[Category: Metal binding protein-protein binding complex]]
-[[Category: Metal-binding]]
-[[Category: Methylation]]
-[[Category: Munc13]]
-[[Category: Phorbol-ester binding]]
-[[Category: Phosphoprotein]]
-[[Category: Protein]]
-[[Category: Synapse]]
-[[Category: Zinc]]
-[[Category: Zinc-finger]]