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.
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| ID: mdl-39207574
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).
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MEDLINE
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Biomol NMR Assign
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Biomolecular NMR assignments
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Biomolecular NMR assignments (Online)
Asunto de la revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Año:
2024
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Article