7RHK

Cryo-EM structure of human rod CNGA1/B1 channel in L-cis-Diltiazem-trapped closed state

Summary for 7RHK

• Entry DOI: 10.2210/pdb7rhk/pdb
• EMDB information: 24458 24460 24461 24462 24463 24464 24465
• Descriptor: cGMP-gated cation channel alpha-1, Cyclic nucleotide-gated cation channel beta-1, CYCLIC GUANOSINE MONOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: ion channel, transport protein
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 4
• Total formula weight: 286785.94

Authors

Xue, J.,Han, Y.,Jiang, Y. (deposition date: 2021-07-17, release date: 2021-11-03, Last modification date: 2024-06-05)

Primary citation

Xue, J.,Han, Y.,Zeng, W.,Jiang, Y.
Structural mechanisms of assembly, permeation, gating, and pharmacology of native human rod CNG channel.
Neuron, 110:86-95.e5, 2022

PubMed Abstract: Mammalian cyclic nucleotide-gated (CNG) channels are nonselective cation channels activated by cGMP or cAMP and play essential roles in the signal transduction of the visual and olfactory sensory systems. CNGA1, the principal component of the CNG channel from rod photoreceptors, can by itself form a functional homotetrameric channel and has been used as the model system in the majority of rod CNG studies. However, the native rod CNG functions as a heterotetramer consisting of three A1 and one B1 subunits and exhibits different functional properties than the CNGA1 homomer. Here we present the functional analysis of human rod CNGA1/B1 heterotetramer and its cryo-EM structures in apo, cGMP-bound, cAMP-bound, and L-cis-Diltiazem-blocked states. These structures, with resolution ranging from 2.6 to 3.3 Å, elucidate the structural mechanisms underlying the 3:1 subunit stoichiometry, the asymmetrical gating upon cGMP activation, and the unique pharmacological property of the native rod CNG channel.

PubMed: 34699778
DOI: 10.1016/j.neuron.2021.10.006

Experimental method

ELECTRON MICROSCOPY (3.27 Å)