Chemical shift assignments of calmodulin bound to a C-terminal site (residues 1120–1147) in the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1)
| Autor: | Aritra Bej, James B. Ames |
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| Rok vydání: | 2022 |
| Předmět: |
CNGB1
Cyclic CaM Photoreceptor Nucleotides Nuclear Magnetic Resonance Neurosciences Biophysics Cyclic Nucleotide-Gated Cation Channels Biochemistry NMR Retina Protein Subunits Calmodulin Retinal Rod Photoreceptor Cells Structural Biology Humans Calcium Biochemistry and Cell Biology Nucleotides Cyclic Nuclear Magnetic Resonance Biomolecular Biomolecular |
| Zdroj: | Biomolecular NMR assignments, vol 16, iss 2 |
| ISSN: | 1874-270X 1874-2718 |
| Popis: | Retinal cyclic nucleotide-gated (CNG) channels consist of two protein subunits (CNGA1 and CNGB1). Calmodulin (CaM) binds to two separate sites within the cytosolic region of CNGB1: CaM binding to an N-terminal site (human CNGB1 residues 565–587, called CaM1) decreases the open probability of CNG channels at elevated Ca2+ levels in dark-adapted photoreceptors, whereas CaM binding to a separate C-terminal site (CNGB1 residues 1120–1147, called CaM2) may increase channel open probability in light activated photoreceptors. We recently reported NMR chemical shift assignments of Ca2+-saturated CaM bound to the CaM1 site of CNGB1 (BMRB no. 51222). Here, we report complete NMR chemical shift assignments of Ca2+-saturated CaM bound to the C-terminal CaM2 site of CNGB1 (BMRB no. 51447). |
| Databáze: | OpenAIRE |
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