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Structure paper

TitleCryo-EM structures of the triheteromeric NMDA receptor and its allosteric modulation.
Journal, issue, pagesScience, Vol. 355, Issue 6331, Year 2017
Publish date2017--24
AuthorsWei Lü / Juan Du / April Goehring / Eric Gouaux
External linksPubMed:28232581 / Publisher's page
MethodsEM (single particle)
Resolution4.5 - 6 A
Structure data

EMDB-8579:
Triheteromeric NMDA receptor GluN1/GluN2A/GluN2B in complex with glycine, glutamate, MK-801 and a GluN2B-specific Fab, at pH 6.5

EMDB-8580:
membrane protein

EMDB-8581:
Triheteromeric NMDA receptor GluN1/GluN2A/GluN2B in complex with glycine, glutamate, Ro 25-6981, MK-801 and a GluN2B-specific Fab, at pH 6.5

EMDB-8583:
membrane protein

PDB-5uow:
Triheteromeric NMDA receptor GluN1/GluN2A/GluN2B in complex with glycine, glutamate, MK-801 and a GluN2B-specific Fab, at pH 6.5

PDB-5up2:
Triheteromeric NMDA receptor GluN1/GluN2A/GluN2B in complex with glycine, glutamate, Ro 25-6981, MK-801 and a GluN2B-specific Fab, at pH 6.5

Chemicals

ChemComp-NAG:
N-ACETYL-D-GLUCOSAMINE

ChemComp-GLU:
GLUTAMIC ACID

ChemComp-BMK:
(5S,10R)-5-methyl-10,11-dihydro-5H-5,10-epiminodibenzo[a,d][7]annulene

SourceXenopus laevis / amphibia / African clawed frog /
Mus musculus / mammal / ハツカネズミ, はつかねずみ /
KeywordsAllosteric Regulation / Animals / Antibodies, Monoclonal / Cryoelectron Microscopy / Models, Molecular / N-methyl D-aspartate receptor subtype 2A / NR1 protein, Xenopus / NR2B NMDA receptor / Neuronal Plasticity / Protein Domains / Protein Multimerization / Receptors, Glutamate / Receptors, N-Methyl-D-Aspartate / Xenopus Proteins / Xenopus laevis / MEMBRANE PROTEIN / membrane protein

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Oct 4, 2017. Three pioneers of this field were awarded Nobel Prize in Chemistry 2017

Three pioneers of this field were awarded Nobel Prize in Chemistry 2017

  • Jacques Dubochet (University of Lausanne, Switzerland) is a pioneer of ice-embedding method of EM specimen (as known as cryo-EM), Most of 3DEM structures in EMDB and PDB are obtained using his method.
  • Joachim Frank (Columbia University, New York, USA) is a pioneer of single particle reconstruction, which is the most used reconstruction method for 3DEM structures in EMDB and EM entries in PDB. And also, he is a develper of Spider, which is one of the most famous software in this field, and is used for some EM Navigor data (e.g. map projection/slice images).
  • Richard Henderson (MRC Laboratory of Molecular Biology, Cambridge, UK) was determined the first biomolecule structure by EM. The first EM entry in PDB, PDB-1brd is determinedby him.

External links: The 2017 Nobel Prize in Chemistry - Press Release

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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

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Sep 15, 2016. EM Navigator & Yorodumi renewed

EM Navigator & Yorodumi renewed

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Aug 31, 2016. New EM Navigator & Yorodumi

New EM Navigator & Yorodumi

  • In 15th Sep 2016, the development versions of EM Navigator and Yorodumi will replace the official versions.
  • Current version will continue as 'legacy version' for some time.

Related info.: Changes in new EM Navigator and Yorodumi / EM Navigator / Yorodumi / EM Navigator (legacy version) / Yorodumi (legacy version)

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EMN Papers

Database of articles cited by 3DEM data entries

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