[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

TitleArchitecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM.
Journal, issue, pagesScience, Vol. 364, Issue 6438, Page 355-362, Year 2019
Publish dateApr 26, 2019
AuthorsYan Zhao / Shanshuang Chen / Adam C Swensen / Wei-Jun Qian / Eric Gouaux /
PubMed AbstractGlutamate-gated AMPA receptors mediate the fast component of excitatory signal transduction at chemical synapses throughout all regions of the mammalian brain. AMPA receptors are tetrameric ...Glutamate-gated AMPA receptors mediate the fast component of excitatory signal transduction at chemical synapses throughout all regions of the mammalian brain. AMPA receptors are tetrameric assemblies composed of four subunits, GluA1-GluA4. Despite decades of study, the subunit composition, subunit arrangement, and molecular structure of native AMPA receptors remain unknown. Here we elucidate the structures of 10 distinct native AMPA receptor complexes by single-particle cryo-electron microscopy (cryo-EM). We find that receptor subunits are arranged nonstochastically, with the GluA2 subunit preferentially occupying the B and D positions of the tetramer and with triheteromeric assemblies comprising a major population of native AMPA receptors. Cryo-EM maps define the structure for S2-M4 linkers between the ligand-binding and transmembrane domains, suggesting how neurotransmitter binding is coupled to ion channel gating.
External linksScience / PubMed:30975770 / PubMed Central
MethodsEM (single particle)
Resolution4.5 - 32 Å
Structure data

EMDB-0426:
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM
Method: EM (single particle) / Resolution: 12.8 Å

EMDB-0427:
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM
Method: EM (single particle) / Resolution: 22 Å

EMDB-0428:
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM
Method: EM (single particle) / Resolution: 32 Å

EMDB-0429:
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM
Method: EM (single particle) / Resolution: 12.8 Å

EMDB-0430:
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM
Method: EM (single particle) / Resolution: 8.7 Å

EMDB-0431:
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM
Method: EM (single particle) / Resolution: 23 Å

EMDB-0432:
Architecture and subunit arrangement of native AMPA receptors elucidated by cryo-EM
Method: EM (single particle) / Resolution: 21 Å

EMDB-20085:
structure of a complex
Method: EM (single particle) / Resolution: 4.5 Å

EMDB-9387, PDB-6njl:
structure of a complex
Method: EM (single particle) / Resolution: 6.7 Å

EMDB-9388, PDB-6njm:
structure of a complex
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-9389, PDB-6njn:
structure of a complex
Method: EM (single particle) / Resolution: 6.5 Å

Chemicals

ChemComp-ZK1:
{[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid / antagonist, medication*YM / Fanapanel

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

Source
  • rattus norvegicus (Norway rat)
  • Rat (rat)
  • mus musculus (house mouse)
KeywordsAnimals / Brain / Cryoelectron Microscopy / Ion Channel Gating / Protein Conformation / Protein Multimerization / Protein Subunits / Rats / Receptors, AMPA / Single Molecule Imaging / MEMBRANE PROTEIN/IMMUNE SYSTEM / AMPA receptor / ligand gated ion channel / neurotransmitter / synapse / MEMBRANE PROTEIN / MEMBRANE PROTEIN-IMMUNE SYSTEM complex

+
About Yorodumi Papers

-
News

-
Aug 12, 2020. New: Covid-19 info

New: Covid-19 info

  • 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. New: 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. (see PDBe EMDB page)
  • 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 at PDBe / 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. See below links for details.
  • 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

+
Jun 16, 2017. Omokage search with filter

Omokage search with filter

  • Result of Omokage search can be filtered by keywords and the database types

Related info.:Omokage search

Read more

-
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