Journal
NEURON
Volume 33, Issue 5, Pages 703-713Publisher
CELL PRESS
DOI: 10.1016/S0896-6273(02)00599-8
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Funding
- NEI NIH HHS [EY01730, R01 EY13007] Funding Source: Medline
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In cyclic nucleotide-gated (CNG) ion channels, binding of cGMP or cAMP drives a conformational change that leads to opening of an ion-conducting pore. One region implicated in the coupling of ligand binding to opening of the pore is the C linker region. Here, we used crosslinking of endogenous cysteines to study interregion proximity. We demonstrate that an individual amino acid-C481-in the C linker region of each of two neighboring subunits can form a disulfide bond. Further, using tandem dimers, we show that a disulfide bond between C35 in the N-terminal region and C481 in the C linker region can form either within a subunit or between subunits. From our data on proximity between individual amino acids and previous studies, a picture emerges of the C linker as a potential dimerization interface.
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