5j7j
From Proteopedia
(Difference between revisions)
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==NMR Derived Structure of Ca2+ Calmodulin bound to Phosphorylated PSD-95== | ==NMR Derived Structure of Ca2+ Calmodulin bound to Phosphorylated PSD-95== | ||
| - | <StructureSection load='5j7j' size='340' side='right' caption='[[5j7j]], [[NMR_Ensembles_of_Models | 4 NMR models]]' scene=''> | + | <StructureSection load='5j7j' size='340' side='right'caption='[[5j7j]], [[NMR_Ensembles_of_Models | 4 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5j7j]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5J7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J7J FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j7j]] 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=5J7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5J7J 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TPO:PHOSPHOTHREONINE'>TPO</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mes|2mes]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2mes|2mes]]</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='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=5j7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j7j OCA], [http://pdbe.org/5j7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j7j RCSB], [http://www.ebi.ac.uk/pdbsum/5j7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j7j ProSAT]</span></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=5j7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j7j OCA], [http://pdbe.org/5j7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j7j RCSB], [http://www.ebi.ac.uk/pdbsum/5j7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j7j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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/DLG4_HUMAN DLG4_HUMAN]] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B (By similarity). | [[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/DLG4_HUMAN DLG4_HUMAN]] Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Postsynaptic density protein-95 (PSD-95) localizes AMPA-type glutamate receptors (AMPARs) to postsynaptic sites of glutamatergic synapses. Its postsynaptic displacement is necessary for loss of AMPARs during homeostatic scaling down of synapses. Here, we demonstrate that upon Ca(2+) influx, Ca(2+)/calmodulin (Ca(2+)/CaM) binding to the N-terminus of PSD-95 mediates postsynaptic loss of PSD-95 and AMPARs during homeostatic scaling down. Our NMR structural analysis identified E17 within the PSD-95 N-terminus as important for binding to Ca(2+)/CaM by interacting with R126 on CaM. Mutating E17 to R prevented homeostatic scaling down in primary hippocampal neurons, which is rescued via charge inversion by ectopic expression of CaM(R)(126E), as determined by analysis of miniature excitatory postsynaptic currents. Accordingly, increased binding of Ca(2+)/CaM to PSD-95 induced by a chronic increase in Ca(2+) influx is a critical molecular event in homeostatic downscaling of glutamatergic synaptic transmission. | ||
| + | |||
| + | Ca(2+)/calmodulin binding to PSD-95 mediates homeostatic synaptic scaling down.,Chowdhury D, Turner M, Patriarchi T, Hergarden AC, Anderson D, Zhang Y, Sun J, Chen CY, Ames JB, Hell JW EMBO J. 2018 Jan 4;37(1):122-138. doi: 10.15252/embj.201695829. Epub 2017 Nov 8. PMID:29118000<ref>PMID:29118000</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5j7j" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Calmodulin 3D structures|Calmodulin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: African clawed frog]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Ames, J B]] | [[Category: Ames, J B]] | ||
[[Category: Anderson, D E]] | [[Category: Anderson, D E]] | ||
Revision as of 13:04, 10 May 2019
NMR Derived Structure of Ca2+ Calmodulin bound to Phosphorylated PSD-95
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