Chemical shift assignments of the α-actinin C-terminal EF-hand domain bound to a cytosolic C0 domain of GluN1 (residues 841-865) from the NMDA receptor

Aritra Bej; Johannes W Hell; James B Ames

doi:10.1007/s12104-024-10194-2

Chemical shift assignments of the α-actinin C-terminal EF-hand domain bound to a cytosolic C0 domain of GluN1 (residues 841-865) from the NMDA receptor

Biomol NMR Assign. 2024 Aug 29. doi: 10.1007/s12104-024-10194-2. Online ahead of print.

Authors

Aritra Bej¹, Johannes W Hell², James B Ames³

Affiliations

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

PMID: 39207574
DOI: 10.1007/s12104-024-10194-2

Abstract

N-methyl-D-aspartate receptors (NMDARs) consist of glycine-binding GluN1 and glutamate-binding GluN2 subunits that form tetrameric ion channels. NMDARs in the brain are important for controlling neuronal excitability to promote synaptic plasticity. The cytoskeletal protein, α-actinin-1 (100 kDa, called ACTN1) binds to the cytosolic C0 domain of GluN1 (residues 841-865) that may play a role in the Ca²⁺-dependent desensitization of NMDAR channels. Mutations that disrupt NMDAR channel function are linked to Alzheimer's disease, depression, stroke, epilepsy, and schizophrenia. NMR chemical shift assignments are reported here for the C-terminal EF-hand domain of ACTN1 (residues 824-892, called ACTN_EF34) and ACTN_EF34 bound to the GluN1 C0 domain (BMRB numbers 52385 and 52386, respectively).

Keywords: C0 domain; Calcium; GluN1; NMDA receptor; NMR; a-actinin.

Grants and funding

R01-EY012347/EY/NEI NIH HHS/United States