Evidence map›Paper›PMID 37463923›Full record

ArticleNature communications2023

Conformational trajectory of allosteric gating of the human cone photoreceptor cyclic nucleotide-gated channel.

Zhengshan Hu, Xiangdong Zheng, Jian Yang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 17% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. High-Throughput MicroED for Probing Ion Channel Dynamics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Article
  7. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Zhengshan HuDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Xiangdong ZhengDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA.
Jian YangDepartment of Biological Sciences, Columbia University, New York, NY, 10027, USA. jy160@columbia.edu.ORCID 0000-0003-0290-7688
Columbia University · US

Funding

NCCAT: National Center for CryoEM Access and Training- Supplement for Windows 10 and FFIU24GM129539 · NIGMS · NEW YORK STRUCTURAL BIOLOGY CENTER · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2018 to 2023
$53.9M
TRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7M
TRPML1 channel physiology and pathophysiologyR01GM085234 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI YANG, JIAN · 2009 to 2022
$4.2M
Molecular physiology and biophysics of cyclic nucleotide-gated channelsR01EY032880 · NEI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI TONG, LIANG · 2022 to 2025
$1.9M
Acquisition of Detector for JEOL 3200 FSC Electron MicroscopeS10OD019994 · OD · NEW YORK STRUCTURAL BIOLOGY CENTER · PI CARRAGHER, BRIDGET OLIVIA · 2015 to 2015
$600k
NEI NIH HHS R01 EY032880NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01 GM085234NIGMS NIH HHS U24 GM129539NIH HHS S10 OD019994
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) channels transduce chemical signals into electrical signals in sensory receptors and neurons. They are activated by cGMP or cAMP, which bind to the cyclic nucleotide-binding domain (CNBD) to open a gate located 50-60 Å away in the central cavity. Structures of closed and open vertebrate CNG channels have been solved, but the conformational landscape of this allosteric gating remains to be elucidated and enriched. Here, we report structures of the cGMP-activated human cone photoreceptor CNGA3/CNGB3 channel in closed, intermediate, pre-open and open states in detergent or lipid nanodisc, all with fully bound cGMP. The pre-open and open states are obtained only in the lipid nanodisc, suggesting a critical role of lipids in tuning the energetic landscape of CNGA3/CNGB3 activation. The different states exhibit subunit-unique, incremental and distinct conformational rearrangements that originate in the CNBD, propagate through the gating ring to the transmembrane domain, and gradually open the S6 cavity gate. Our work illustrates a spatial conformational-change wave of allosteric gating of a vertebrate CNG channel by its natural ligand and provides an expanded framework for studying CNG properties and channelopathy.

Indexed as

Cyclic Nucleotide-Gated Cation ChannelsRetinal Cone Photoreceptor CellsCyclic GMPHumansLipidsMolecular ConformationNucleotides, CyclicCyclic GMPCyclic Nucleotide-Gated Cation ChannelsLipidsNucleotides, Cyclic

Identifiers

PMID37463923
PMCPMC10354024
OpenAlexW4384662812

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.