Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004–1024) from the NMDA receptor
Author:
Funder
National Eye Institute
Publisher
Springer Science and Business Media LLC
Subject
Biochemistry,Structural Biology
Link
https://link.springer.com/content/pdf/10.1007/s12104-023-10125-7.pdf
Reference32 articles.
1. Babu YS, Bugg CE, Cook WJ (1988) Structure of calmodulin refined at 2.2 A resolution. J Mol Biol 204:191–204
2. Bajaj G, Hau AM, Hsu P, Gafken PR, Schimerlik MI, Ishmael JE (2014) Identification of an atypical calcium-dependent calmodulin binding site on the C-terminal domain of GluN2A. Biochem Biophys Res Commun 444:588–594
3. Bej A, Ames JB (2022a) Chemical shift assignments of calmodulin bound to the beta-subunit of a retinal cyclic nucleotide-gated channel (CNGB1). Biomol NMR Assign 16:147–151
4. Bej A, Ames JB (2022b) Chemical shift assignments of calmodulin under standard conditions at neutral pH. Biomol NMR Assign 16:213–218
5. Bej A, Ames JB (2022c) NMR structures of calmodulin bound to two separate regulatory sites in the retinal cyclic nucleotide-gated channel. Biochemistry 61:1955–1965
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