PDBsum entry 2mes

Metal binding protein

PDB id: 2mes

Contents

Protein chains

144 a.a.

19 a.a.

Metals

_CA ×4

PDB id:

2mes

Name:

Metal binding protein

Title:

Backbone 1h, 13c, 15n resonance assignments of calcium-bound calmodulin in complex with psd95 n-terminal peptide

Structure:

Calmodulin. Chain: a. Synonym: cam. Engineered: yes. Disks large homolog 4. Chain: b. Fragment: unp residues 1-71. Synonym: postsynaptic density protein 95, psd-95, synapse-associated protein 90, sap-90, sap90.

Source:

Xenopus laevis. Clawed frog,common platanna,platanna. Organism_taxid: 8355. Gene: calm1, calm2. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606.

NMR struc:

10 models

Authors:

Y.Zhang,J.B.Ames

Key ref:

Y.Zhang et al. (2014). Capping of the N-terminus of PSD-95 by calmodulin triggers its postsynaptic release. Embo J, 33, 1341-1353. PubMed id: 24705785 DOI: 10.1002/embj.201488126

Date:

26-Sep-13 Release date: 24-Dec-14

Protein chain

No UniProt id for this chain

Struc: 144 a.a.

Protein chain

P78352  (DLG4_HUMAN) -  Disks large homolog 4 from Homo sapiens

Seq: 724 a.a.

Struc: 19 a.a.

Enzyme reactions

• Enzyme class: Chain B: E.C.?

DOI no: 10.1002/embj.201488126

Embo J 33:1341-1353 (2014)

PubMed id: 24705785

Capping of the N-terminus of PSD-95 by calmodulin triggers its postsynaptic release.

Y.Zhang, L.Matt, T.Patriarchi, Z.A.Malik, D.Chowdhury, D.K.Park, A.Renieri, J.B.Ames, J.W.Hell.

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.