PDBsum entry 4u1x

Transport protein, membrane protein

PDB id: 4u1x

Contents

Protein chains

743 a.a.

Ligands

KAI ×4

NAG ×4

FWF ×2

MES

PDB id:

4u1x

Name:

Transport protein, membrane protein

Title:

Full length glua2-kainate-(r,r)-2b complex crystal form b

Structure:

Glutamate receptor 2. Chain: a, b, c, d. Synonym: glur-2,ampa-selective glutamate receptor 2,glur-b,glur-k2, glutamate receptor ionotropic,ampa 2,glua2. Engineered: yes

Source:

Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: gria2, glur2. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: ric15

Resolution:

3.30Å R-factor: 0.245 R-free: 0.289

Authors:

L.Chen,E.Gouaux

Key ref:

K.L.Dürr et al. (2014). Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states. Cell, 158, 778-792. PubMed id: 25109876 DOI: 10.1016/j.cell.2014.07.023

Date:

16-Jul-14 Release date: 20-Aug-14

Protein chains

P19491  (GRIA2_RAT) -  Glutamate receptor 2 from Rattus norvegicus

Seq: 883 a.a.

Struc: 743 a.a.*

* PDB and UniProt seqs differ at 13 residue positions (black crosses)

DOI no: 10.1016/j.cell.2014.07.023

Cell 158:778-792 (2014)

PubMed id: 25109876

Structure and dynamics of AMPA receptor GluA2 in resting, pre-open, and desensitized states.

K.L.Dürr, L.Chen, R.A.Stein, R.De Zorzi, I.M.Folea, T.Walz, H.S.Mchaourab, E.Gouaux.

ABSTRACT

Ionotropic glutamate receptors (iGluRs) mediate the majority of fast excitatory signaling in the nervous system. Despite the profound importance of iGluRs to neurotransmission, little is known about the structures and dynamics of intact receptors in distinct functional states. Here, we elucidate the structures of the intact GluA2 AMPA receptor in an apo resting/closed state, in an activated/pre-open state bound with partial agonists and a positive allosteric modulator, and in a desensitized/closed state in complex with fluorowilliardiine. To probe the conformational properties of these states, we carried out double electron-electron resonance experiments on cysteine mutants and cryoelectron microscopy studies. We show how agonist binding modulates the conformation of the ligand-binding domain "layer" of the intact receptors and how, upon desensitization, the receptor undergoes large conformational rearrangements of the amino-terminal and ligand-binding domains. We define mechanistic principles by which to understand antagonism, activation, and desensitization in AMPA iGluRs.