Dataset Information
Cryo-EM structure of human rod CNGA1 channel in apo-state
Ontology highlight
ABSTRACT:
SUBMITTER: Youxing Jiang
PROVIDER: EMPIAR-10722 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structural mechanisms of gating and selectivity of human rod CNGA1 channel.
Neuron 20210301 8
Mammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand gating in human rod CNGA1 channel by determining its cryo-EM structures in both the apo closed and cGMP-bound open states. Distinct from most other members of voltage-gated tetrameric cation channels, CNGA1 forms a central channel gate in the middle of the membrane, occluding the central cavity. Structura ...[more]