PDBsum entry 4tll

Signaling protein

PDB id: 4tll

Contents

Protein chains

767 a.a.

738 a.a.

719 a.a.

Ligands

NAG ×4

1AC

QEM ×2

JEG

PDB id:

4tll

Name:

Signaling protein

Title:

Crystal structure of glun1/glun2b nmda receptor, structure 1

Structure:

Receptor subunit glun1. Chain: a, c. Fragment: unp residues 22-836. Synonym: n-methyl-d-aspartate receptor subunit nr1-8a. Engineered: yes. Mutation: yes. Receptor subunit glun2b. Chain: b, d. Fragment: unp residues 20-839.

Source:

Xenopus laevis. African clawed frog. Organism_taxid: 8355. Expressed in: homo sapiens. Expression_system_taxid: 9606. Gene: nr2b. Expression_system_taxid: 9606

Resolution:

3.59Å R-factor: 0.268 R-free: 0.305

Authors:

E.Gouaux,C.-H.Lee,W.Lu

Key ref:

C.H.Lee et al. (2014). NMDA receptor structures reveal subunit arrangement and pore architecture. Nature, 511, 191-197. PubMed id: 25008524 DOI: 10.1038/nature13548

Date:

30-May-14 Release date: 02-Jul-14

Protein chain

A0A1L8F5J9  (NMDZ1_XENLA) -  Glutamate receptor ionotropic, NMDA 1 from Xenopus laevis

Seq: 903 a.a.

Struc: 767 a.a.*

Protein chains

A7XY94  (NMDE2_XENLA) -  Glutamate receptor ionotropic, NMDA 2B from Xenopus laevis

Seq: 1448 a.a.

Struc: 738 a.a.*

Protein chain

A0A1L8F5J9  (NMDZ1_XENLA) -  Glutamate receptor ionotropic, NMDA 1 from Xenopus laevis

Seq: 903 a.a.

Struc: 719 a.a.*

* PDB and UniProt seqs differ at 35 residue positions (black crosses)

DOI no: 10.1038/nature13548

Nature 511:191-197 (2014)

PubMed id: 25008524

NMDA receptor structures reveal subunit arrangement and pore architecture.

C.H.Lee, W.Lü, J.C.Michel, A.Goehring, J.Du, X.Song, E.Gouaux.

ABSTRACT

N-methyl-d-aspartate (NMDA) receptors are Hebbian-like coincidence detectors, requiring binding of glycine and glutamate in combination with the relief of voltage-dependent magnesium block to open an ion conductive pore across the membrane bilayer. Despite the importance of the NMDA receptor in the development and function of the brain, a molecular structure of an intact receptor has remained elusive. Here we present X-ray crystal structures of the Xenopus laevis GluN1-GluN2B NMDA receptor with the allosteric inhibitor, Ro25-6981, partial agonists and the ion channel blocker, MK-801. Receptor subunits are arranged in a 1-2-1-2 fashion, demonstrating extensive interactions between the amino-terminal and ligand-binding domains. The transmembrane domains harbour a closed-blocked ion channel, a pyramidal central vestibule lined by residues implicated in binding ion channel blockers and magnesium, and a ∼twofold symmetric arrangement of ion channel pore loops. These structures provide new insights into the architecture, allosteric coupling and ion channel function of NMDA receptors.