[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleStructural mechanisms of assembly, permeation, gating, and pharmacology of native human rod CNG channel.
Journal, issue, pagesNeuron, Vol. 110, Issue 1, Page 86-95.e5, Year 2022
Publish dateJan 5, 2022
AuthorsJing Xue / Yan Han / Weizhong Zeng / Youxing Jiang /
PubMed AbstractMammalian 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 ...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.
External linksNeuron / PubMed:34699778 / PubMed Central
MethodsEM (single particle)
Resolution2.61 - 3.31 Å
Structure data

EMDB-24458, PDB-7rh9:
Cryo-EM structure of human rod CNGA1/B1 channel in apo state
Method: EM (single particle) / Resolution: 2.61 Å

EMDB-24460, PDB-7rhg:
Cryo-EM structure of human rod CNGA1/B1 channel in cAMP-bound state
Method: EM (single particle) / Resolution: 2.88 Å

EMDB-24461, PDB-7rhh:
Cryo-EM structure of human rod CNGA1/B1 channel in cGMP-bound openI state
Method: EM (single particle) / Resolution: 3.31 Å

EMDB-24462, PDB-7rhi:
Cryo-EM structure of human rod CNGA1/B1 channel in cGMP-bound openII state
Method: EM (single particle) / Resolution: 3.31 Å

EMDB-24463, PDB-7rhj:
Cryo-EM structure of human rod CNGA1/B1 channel in L-cis-Diltiazem-blocked open state
Method: EM (single particle) / Resolution: 2.88 Å

EMDB-24464, PDB-7rhk:
Cryo-EM structure of human rod CNGA1/B1 channel in L-cis-Diltiazem-trapped closed state
Method: EM (single particle) / Resolution: 3.27 Å

EMDB-24465, PDB-7rhl:
Cryo-EM structure of human rod Apo CNGA1/B1 channel with CLZ coiled coil
Method: EM (single particle) / Resolution: 3.03 Å

Chemicals

ChemComp-CMP:
ADENOSINE-3',5'-CYCLIC-MONOPHOSPHATE

ChemComp-PCG:
CYCLIC GUANOSINE MONOPHOSPHATE

ChemComp-5H0:
(2R,3R)-5-[2-(dimethylamino)ethyl]-2-(4-methoxyphenyl)-4-oxo-2,3,4,5-tetrahydro-1,5-benzothiazepin-3-yl acetate

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / ion channel

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more