Evidence map›Paper›PMID 28099415›Full record

ArticleNature2017

Structure of a eukaryotic cyclic-nucleotide-gated channel.

Minghui Li, Xiaoyuan Zhou, Shu Wang, Ioannis Michailidis, Ye Gong, Deyuan Su, Huan Li, Xueming Li, Jian Yang

Abstract read
In one paragraph

Article in Nature, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
10.4field-weighted citation impact, top 1% 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

101 citing papers in PubMed, 168 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. cAMP binding to closed pacemaker ion channels is cooperative.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
  20. Article

41 more citing papers are in PubMed but not listed here.

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

9 authors at 4 institutions in 2 countries.

Minghui LiDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Xiaoyuan ZhouBeijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Shu WangKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences, Kunming 650223, China.
Ioannis MichailidisDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Ye GongKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences, Kunming 650223, China.
Deyuan SuKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences, Kunming 650223, China.
Huan LiKey Laboratory of Animal Models and Human Disease Mechanisms of the Chinese Academy of Sciences, Chinese Academy of Sciences, Kunming 650223, China.
Xueming LiBeijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.
Jian YangDepartment of Biological Sciences, Columbia University, New York, New York 10027, USA.
Kunming Institute of Zoology · CNCenter for Life Sciences · CNColumbia University · USChinese Academy of Sciences · CN

Funding

TRPML1 channel physiology and pathophysiologyR01GM085234 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI YANG, JIAN · 2009 to 2022
$4.2M
Structural basis of Ca2+ channel function and regulationR01NS053494 · NINDS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI YANG, JIAN · 2007 to 2015
$3.2M
NIGMS NIH HHS R01 GM085234NINDS NIH HHS R01 NS053494
6 · The paper itself

Abstract

Cyclic-nucleotide-gated channels are essential for vision and olfaction. They belong to the voltage-gated ion channel superfamily but their activities are controlled by intracellular cyclic nucleotides instead of transmembrane voltage. Here we report a 3.5-Å-resolution single-particle electron cryo-microscopy structure of a cyclic-nucleotide-gated channel from Caenorhabditis elegans in the cyclic guanosine monophosphate (cGMP)-bound open state. The channel has an unusual voltage-sensor-like domain, accounting for its deficient voltage dependence. A carboxy-terminal linker connecting S6 and the cyclic-nucleotide-binding domain interacts directly with both the voltage-sensor-like domain and the pore domain, forming a gating ring that couples conformational changes triggered by cyclic nucleotide binding to the gate. The selectivity filter is lined by the carboxylate side chains of a functionally important glutamate and three rings of backbone carbonyls. This structure provides a new framework for understanding mechanisms of ion permeation, gating and channelopathy of cyclic-nucleotide-gated channels and cyclic nucleotide modulation of related channels.

Indexed as

Caenorhabditis elegansCryoelectron MicroscopyAmino Acid SequenceAnimalsCaenorhabditis elegans ProteinsCyclic GMPCyclic Nucleotide-Gated Cation ChannelsElectric ConductivityGlutamic AcidIon Channel GatingIon ChannelsModels, BiologicalModels, MolecularProtein DomainsCaenorhabditis elegans ProteinsCyclic GMPCyclic Nucleotide-Gated Cation ChannelsGlutamic AcidIon Channelstax-4 protein, C elegans

Identifiers

PMID28099415
PMCPMC5783306
OpenAlexW2572480523

What OpenQuestion holds

Textmetadata
LicenceTDM
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.