title: Chemical shift assignments of the C-terminal EF-hand domain of α-actinin-1.
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).
authors: Department of Chemistry, University of California, Davis, Davis, CA, 95616, USA.
authors: Matthew
authors: M
authors: Turner
authors: Department of Chemistry, University of California, Davis, Davis, CA, 95616, USA.
authors: David E
authors: DE
authors: Anderson
authors: Department of Chemistry, University of California, Davis, Davis, CA, 95616, USA.
authors: Sahana
authors: S
authors: Rajan
authors: Department of Pharmacology, University of California, Davis, Davis, CA, 95616, USA.
authors: Johannes W
authors: JW
authors: Hell
authors: Department of Chemistry, University of California, Davis, Davis, CA, 95616, USA. jbames@ucdavis.edu.
authors: James B
authors: JB
authors: Ames
mesh_terms: D000185:Actinin / Q000737:chemistry*; D000595:Amino Acid Sequence; D020832:EF Hand Motifs; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular
chemical_list: C526905:ACTN1 protein, human; D000185:Actinin
keywords: CaV1.2; EF-hand; IQ-motif; Long-term depression; Synaptic plasticity; α-Actinin-1