Chemical shift assignments of a calmodulin intermediate with two Ca2+ bound in complex with the IQ-motif of voltage-gated Ca2+ channels (CaV1.2)

Ian Salveson; David E Anderson; Johannes W Hell; James B Ames

doi:10.1007/s12104-019-09883-0

Chemical shift assignments of a calmodulin intermediate with two Ca²⁺ bound in complex with the IQ-motif of voltage-gated Ca²⁺ channels (Ca_V1.2)

Biomol NMR Assign. 2019 Apr;13(1):233-237. doi: 10.1007/s12104-019-09883-0. Epub 2019 Feb 20.

Authors

Ian Salveson¹, David E Anderson¹, Johannes W Hell², James B Ames³

Affiliations

¹ Department of Chemistry, University of California, 95616, Davis, CA, USA.
² Department of Pharmacology, University of California, 95616, Davis, CA, USA.
³ Department of Chemistry, University of California, 95616, Davis, CA, USA. jbames@ucdavis.edu.

Abstract

Calcium-dependent inactivation (CDI) of neuronal voltage-gated Ca²⁺ channels (Ca_V1.2) is important for synaptic plasticity, which is associated with learning and memory. The Ca²⁺-dependent binding of calmodulin (CaM) to Ca_V1.2 is essential for CDI. Here we report NMR assignments for a CaM mutant (D21A/D23A/D25A/E32Q/D57A/D59A/N61A/E68Q, called CaM^EF12) that contains two Ca²⁺ bound at the third and fourth EF-hands (EF3 and EF4) and is bound to the IQ-motif (residues 1644-1665) from Ca_V1.2 (BMRB accession no. 27692).

Keywords: CDI; CaV1.2; Calmodulin; EF-hand; IQ-motif; Synaptic plasticity.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Amides / chemistry
Amino Acid Motifs
Calcium / metabolism*
Calcium Channels / chemistry*
Calmodulin / chemistry*
Humans
Nuclear Magnetic Resonance, Biomolecular*
Protein Binding
Protein Structure, Secondary

Substances

Amides
Calcium Channels
Calmodulin
Calcium

Abstract

Publication types

MeSH terms

Substances

Grants and funding