Evidence map›Paper›PMID 32483338›Full record

ArticleNature structural & molecular biology2020

Mechanism of ligand activation of a eukaryotic cyclic nucleotide-gated channel.

Xiangdong Zheng, Ziao Fu, Deyuan Su, Yuebin Zhang, Minghui Li, Yaping Pan, Huan Li, Shufang Li, Robert A Grassucci, Zhenning Ren and 6 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 59 citations in OpenAlex.

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  13. The open gate of the AMPA receptor forms a CaNature structural & molecular biology · 2024
    Article
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  15. Review
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  18. Structural basis of calmodulin modulation of the rod cyclic nucleotide-gated channel.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  19. Review
  20. Article
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

16 authors at 7 institutions in 2 countries.

Xiangdong Zheng *Department of Biological Sciences, Columbia University, New York, NY, USA.
Ziao Fu *Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.ORCID http://orcid.org/0000-0001-5036-1945
Deyuan Su *Key Laboratory of Animal Models and Human Disease Mechanisms of Chinese Academy of Sciences/Key Laboratory of Bioactive Peptides of Yunnan Province, Chinese Academy of Sciences, Kunming, China.
Yuebin ZhangState Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China.
Minghui LiDepartment of Biological Sciences, Columbia University, New York, NY, USA.
Yaping PanDepartment of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
Huan LiDepartment of Biological Sciences, Columbia University, New York, NY, USA.
Shufang LiDepartment of Biological Sciences, Columbia University, New York, NY, USA.
Robert A GrassucciDepartment of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, USA.
Zhenning RenDepartment of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
Zhengshan HuDepartment of Biological Sciences, Columbia University, New York, NY, USA.
Xueming LiBeijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing, China.
Ming ZhouDepartment of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.ORCID http://orcid.org/0000-0001-7198-165X
Guohui LiState Key Laboratory of Molecular Reaction Dynamics, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, Dalian, China. ghli@dicp.ac.cn.ORCID http://orcid.org/0000-0001-8223-705X
Joachim FrankDepartment of Biological Sciences, Columbia University, New York, NY, USA. jf2192@cumc.columbia.edu.ORCID http://orcid.org/0000-0001-5449-6943
Jian YangDepartment of Biological Sciences, Columbia University, New York, NY, USA. jy160@columbia.edu.ORCID http://orcid.org/0000-0003-0290-7688
Columbia University · USBaylor College of Medicine · USDalian Institute of Chemical Physics · CNKunming Institute of Zoology · CNCenter for Life Sciences · CNColumbia University Irving Medical Center · USHarbin Institute of Technology · CN

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
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI GONZALEZ, ANA M · 1985 to 2011
$38.9M
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
Time-resolved Cryo-EM of Short-lived States in Eukaryotic TranslationR01GM055440 · NIGMS · WADSWORTH CENTER · PI FRANK, JOACHIM · 1997 to 2020
$5.1M
TRPML1 channel physiology and pathophysiologyR01GM085234 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI YANG, JIAN · 2009 to 2022
$4.2M
Molecular physiology of cyclic nucleotide-gated channelsR01EY027800 · NEI · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI YANG, JIAN · 2017 to 2019
$1.5M
Acquisition of Detector for JEOL 3200 FSC Electron MicroscopeS10OD019994 · OD · NEW YORK STRUCTURAL BIOLOGY CENTER · PI CARRAGHER, BRIDGET OLIVIA · 2015 to 2015
$600k
NCRR NIH HHS P41 RR001209NEI NIH HHS R01 EY027800NIGMS NIH HHS P41 GM103310NIGMS NIH HHS R01 GM055440NIGMS NIH HHS R01 GM085234NIGMS NIH HHS U24 GM129539NIH HHS S10 OD019994
6 · The paper itself

Abstract

Cyclic nucleotide-gated (CNG) channels convert cyclic nucleotide (CN) binding and unbinding into electrical signals in sensory receptors and neurons. The molecular conformational changes underpinning ligand activation are largely undefined. We report both closed- and open-state atomic cryo-EM structures of a full-length Caenorhabditis elegans cyclic GMP-activated channel TAX-4, reconstituted in lipid nanodiscs. These structures, together with computational and functional analyses and a mutant channel structure, reveal a double-barrier hydrophobic gate formed by two S6 amino acids in the central cavity. cGMP binding produces global conformational changes that open the cavity gate located ~52 Å away but do not alter the structure of the selectivity filter-the commonly presumed activation gate. Our work provides mechanistic insights into the allosteric gating and regulation of CN-gated and nucleotide-modulated channels and CNG channel-related channelopathies.

Indexed as

Caenorhabditis elegans ProteinsCryoelectron MicroscopyCyclic GMPHEK293 CellsHumansHydrophobic and Hydrophilic InteractionsIon ChannelsLigandsLipidsModels, MolecularMolecular Dynamics SimulationMutagenesisMutationProtein ConformationCaenorhabditis elegans ProteinsCyclic GMPIon ChannelsLigandsLipidstax-4 protein, C elegans

Identifiers

PMID32483338
PMCPMC7354226
OpenAlexW3028947668

What OpenQuestion holds

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LicenceTDM
Read underepoch 390

Registered trials

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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.