6FEG

Solution Structure of CaM/Kv7.2-hAB Complex


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the least restraint violations 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural basis and energy landscape for the Ca2+gating and calmodulation of the Kv7.2 K+channel.

Bernardo-Seisdedos, G.Nunez, E.Gomis, C.Malo, C.Villarroel, A.Millet, O.

(2018) Proc Natl Acad Sci U S A 115: 2395-2400

  • DOI: https://doi.org/10.1073/pnas.1800235115
  • Primary Citation of Related Structures:  
    6FEG, 6FEH

  • PubMed Abstract: 

    The Kv7.2 (KCNQ2) channel is the principal molecular component of the slow voltage-gated, noninactivating K + M-current, a key controller of neuronal excitability. To investigate the calmodulin (CaM)-mediated Ca 2+ gating of the channel, we used NMR spectroscopy to structurally and dynamically describe the association of helices h A and h B of Kv7.2 with CaM, as a function of Ca 2+ concentration. The structures of the CaM/Kv7.2-hAB complex at two different calcification states are reported here. In the presence of a basal cytosolic Ca 2+ concentration (10-100 nM), only the N-lobe of CaM is Ca 2+ -loaded and the complex (representative of the open channel) exhibits collective dynamics on the millisecond time scale toward a low-populated excited state (1.5%) that corresponds to the inactive state of the channel. In response to a chemical or electrical signal, intracellular Ca 2+ levels rise up to 1-10 μM, triggering Ca 2+ association with the C-lobe. The associated conformational rearrangement is the key biological signal that shifts populations to the closed/inactive channel. This reorientation affects the C-lobe of CaM and both helices in Kv7.2, allosterically transducing the information from the Ca 2+ -binding site to the transmembrane region of the channel.


  • Organizational Affiliation

    Protein Stability and Inherited Disease Laboratory, Center for Cooperative Research in Biosciences CIC bioGUNE, 48170 Derio, Spain.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Potassium voltage-gated channel subfamily KQT member 2,Potassium voltage-gated channel subfamily KQT member 2115Homo sapiensMutation(s): 0 
Gene Names: KCNQ2
UniProt & NIH Common Fund Data Resources
Find proteins for O43526 (Homo sapiens)
Explore O43526 
Go to UniProtKB:  O43526
PHAROS:  O43526
GTEx:  ENSG00000075043 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO43526
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Calmodulin-1149Homo sapiensMutation(s): 0 
Gene Names: CALM1CALMCAMCAM1
UniProt & NIH Common Fund Data Resources
Find proteins for P0DP23 (Homo sapiens)
Explore P0DP23 
Go to UniProtKB:  P0DP23
PHAROS:  P0DP23
GTEx:  ENSG00000198668 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0DP23
Sequence Annotations
Expand
  • Reference Sequence
Small Molecules
Ligands 1 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
CA
Query on CA

Download Ideal Coordinates CCD File 
C [auth B],
D [auth B]
CALCIUM ION
Ca
BHPQYMZQTOCNFJ-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 10 
  • Selection Criteria: structures with the least restraint violations 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Basque GovernmentSpainElkartek BG2015
Spanish Ministry of Science and TechnologySpainCTQ2015-68756-R, BFU2015-66910-R and CSD2008-00005

Revision History  (Full details and data files)

  • Version 1.0: 2018-02-21
    Type: Initial release
  • Version 1.1: 2018-03-28
    Changes: Data collection, Database references
  • Version 1.2: 2019-05-08
    Changes: Data collection