Chemical shift assignments of the C-terminal EF-hand domain of α-actinin-1

Matthew Turner; David E Anderson; Sahana Rajan; Johannes W Hell; James B Ames

doi:10.1007/s12104-016-9670-2

Chemical shift assignments of the C-terminal EF-hand domain of α-actinin-1

Biomol NMR Assign. 2016 Apr;10(1):219-22. doi: 10.1007/s12104-016-9670-2. Epub 2016 Feb 10.

Authors

Matthew Turner¹, David E Anderson¹, Sahana Rajan¹, Johannes W Hell², James B Ames³

Affiliations

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

Abstract

The regulation and localization of the neuronal voltage gated Ca(2+) channel CaV1.2 is important for synaptic plasticity associated with learning and memory. The cytoskeletal protein, α-actinin-1 is known to interact with CaV1.2 and stabilize its localization at the postsynaptic membrane. Here we report both backbone and sidechain NMR assignments for the C-terminal EF-hands (EF3 and EF4) of α-actinin-1 (residues 824-892, called ACTN_EF34) bound to the IQ-motif (residues 1644-1665) from CaV1.2 (BMRB accession no. 25902).

Keywords: CaV1.2; EF-hand; IQ-motif; Long-term depression; Synaptic plasticity; α-Actinin-1.

Publication types

Research Support, N.I.H., Extramural

MeSH terms

Actinin / chemistry*
Amino Acid Sequence
EF Hand Motifs*
Humans
Nuclear Magnetic Resonance, Biomolecular*

Substances

ACTN1 protein, human
Actinin

Abstract

Publication types

MeSH terms

Substances

Grants and funding