4E53

Calmodulin and Nm peptide complex


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.69 Å
  • R-Value Free: 0.318 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.279 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural basis for the interaction of unstructured neuron specific substrates neuromodulin and neurogranin with calmodulin

Kumar, V.Chichili, V.P.R.Zhong, L.Tang, X.Velazquez-Campoy, A.Sheu, F.-S.Seetharaman, J.Gerges, N.Z.Sivaraman, J.

(2013) Sci Rep 3: 1392-1392

  • DOI: https://doi.org/10.1038/srep01392
  • Primary Citation of Related Structures:  
    4E50, 4E53

  • PubMed Abstract: 

    Neuromodulin (Nm) and neurogranin (Ng) are neuron-specific substrates of protein kinase C (PKC). Their interactions with Calmodulin (CaM) are crucial for learning and memory formation in neurons. Here, we report the structure of IQ peptides (24aa) of Nm/Ng complexed with CaM and their functional studies with full-length proteins. Nm/Ng and their respective IQ peptides are intrinsically unstructured; however, upon binding with CaM, IQ motifs adopt a helical conformation. Ser41 (Ser36) of Nm (Ng) is located in a negatively charged pocket in the apo CaM and, when phosphorylated, it will repel Nm/Ng from CaM. These observations explain the mechanism by which PKC-induced Ser phosphorylation blocks the association of Nm/Ng with CaM and interrupts several learning- and memory-associated functions. Moreover, the present study identified Arg as a key CaM interacting residue from Nm/Ng. This residue is crucial for CaM-mediated function, as evidenced by the inability of the Ng mutant (Arg-to-Ala) to potentiate synaptic transmission in CA1 hippocampal neurons.


  • Organizational Affiliation

    Department of Biological Sciences, National University of Singapore, Singapore.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Calmodulin, Linker, IQ motif of Neuromodulin
A, B
185Mus musculusMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P06837 (Mus musculus)
Explore P06837 
Go to UniProtKB:  P06837
IMPC:  MGI:95639
Find proteins for P0DP26 (Mus musculus)
Explore P0DP26 
Go to UniProtKB:  P0DP26
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupsP0DP26P06837
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.69 Å
  • R-Value Free: 0.318 
  • R-Value Work: 0.276 
  • R-Value Observed: 0.279 
  • Space Group: C 1 2 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 79.386α = 90
b = 79.285β = 90.19
c = 136.064γ = 90
Software Package:
Software NamePurpose
HKL-2000data collection
SHELXSphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-03-20
    Type: Initial release
  • Version 1.1: 2017-06-28
    Changes: Source and taxonomy
  • Version 1.2: 2024-03-20
    Changes: Data collection, Database references