Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 288, Issue 18, Pages 12944-12956Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M113.464123
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Funding
- National Institutes of Health [R01 EY010329, F32EY018981]
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Cyclic nucleotide-regulated ion channels bind second messengers like cAMP to a C-terminal domain, consisting of a beta-roll, followed by two alpha-helices (B- and C-helices). We monitored the cAMP-dependent changes in the structure of the C-helix of a C-terminal fragment of HCN2 channels using transition metal ion FRET between fluorophores on the C-helix and metal ions bound between histidine pairs on the same helix. cAMP induced a change in the dimensions of the C-helix and an increase in the metal binding affinity of the histidine pair. cAMP also caused an increase in the distance between a fluorophore on the C-helix and metal ions bound to the B-helix. Stabilizing the C-helix of intact CNGA1 channels by metal binding to a pair of histidines promoted channel opening. These data suggest that ordering of the C-helix is part of the gating conformational change in cyclic nucleotide-regulated channels.
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