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2MES

Backbone 1H, 13C, 15N resonance assignments of calcium-bound calmodulin in complex with PSD95 N-terminal peptide

Summary for 2MES
Entry DOI10.2210/pdb2mes/pdb
NMR InformationBMRB: 19238
DescriptorCalmodulin, Disks large homolog 4, CALCIUM ION (3 entities in total)
Functional Keywordsprotein/peptide, metal binding protein
Biological sourceXenopus laevis (clawed frog,common platanna,platanna)
More
Cellular locationCell membrane ; Peripheral membrane protein : P78352
Total number of polymer chains2
Total formula weight24880.45
Authors
Zhang, Y.,Ames, J.B. (deposition date: 2013-09-26, release date: 2014-12-24, Last modification date: 2024-05-15)
Primary citationZhang, Y.,Matt, L.,Patriarchi, T.,Malik, Z.A.,Chowdhury, D.,Park, D.K.,Renieri, A.,Ames, J.B.,Hell, J.W.
Capping of the N-terminus of PSD-95 by calmodulin triggers its postsynaptic release.
Embo J., 33:1341-1353, 2014
Cited by
PubMed Abstract: Postsynaptic density protein-95 (PSD-95) is a central element of the postsynaptic architecture of glutamatergic synapses. PSD-95 mediates postsynaptic localization of AMPA receptors and NMDA receptors and plays an important role in synaptic plasticity. PSD-95 is released from postsynaptic membranes in response to Ca(2+) influx via NMDA receptors. Here, we show that Ca(2+)/calmodulin (CaM) binds at the N-terminus of PSD-95. Our NMR structure reveals that both lobes of CaM collapse onto a helical structure of PSD-95 formed at its N-terminus (residues 1-16). This N-terminal capping of PSD-95 by CaM blocks palmitoylation of C3 and C5, which is required for postsynaptic PSD-95 targeting and the binding of CDKL5, a kinase important for synapse stability. CaM forms extensive hydrophobic contacts with Y12 of PSD-95. The PSD-95 mutant Y12E strongly impairs binding to CaM and Ca(2+)-induced release of PSD-95 from the postsynaptic membrane in dendritic spines. Our data indicate that CaM binding to PSD-95 serves to block palmitoylation of PSD-95, which in turn promotes Ca(2+)-induced dissociation of PSD-95 from the postsynaptic membrane.
PubMed: 24705785
DOI: 10.1002/embj.201488126
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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