PDBsum entry 4wxj

Membrane protein

PDB id: 4wxj

Contents

Protein chains

252 a.a.

Ligands

GLU ×2

Waters ×275

PDB id:

4wxj

Name:

Membrane protein

Title:

Drosophila muscle gluriib complex with glutamate

Structure:

Glutamate receptor iib,glutamate receptor iib. Chain: a, b. Fragment: fragment: residues 416-537 and 660-802 were connected by a dipeptide gt linker. Engineered: yes

Source:

Drosophila melanogaster. Fruit fly. Organism_taxid: 7227. Cell: muscle. Gene: gluriib, cg7234, dmel_cg7234. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.199 R-free: 0.230

Authors:

P.Dharkar,M.L.Mayer

Key ref:

T.H.Han et al. (2015). Functional reconstitution of Drosophila melanogaster NMJ glutamate receptors. Proc Natl Acad Sci U S A, 112, 6182-6187. PubMed id: 25918369 DOI: 10.1073/pnas.1500458112

Date:

13-Nov-14 Release date: 29-Apr-15

Protein chains

Q9VMP3  (Q9VMP3_DROME) -  Glutamate receptor IIB from Drosophila melanogaster

Seq: 913 a.a.

Struc: 252 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1073/pnas.1500458112

Proc Natl Acad Sci U S A 112:6182-6187 (2015)

PubMed id: 25918369

Functional reconstitution of Drosophila melanogaster NMJ glutamate receptors.

T.H.Han, P.Dharkar, M.L.Mayer, M.Serpe.

ABSTRACT

The Drosophila larval neuromuscular junction (NMJ), at which glutamate acts as the excitatory neurotransmitter, is a widely used model for genetic analysis of synapse function and development. Despite decades of study, the inability to reconstitute NMJ glutamate receptor function using heterologous expression systems has complicated the analysis of receptor function, such that it is difficult to resolve the molecular basis for compound phenotypes observed in mutant flies. We find that Drosophila Neto functions as an essential component required for the function of NMJ glutamate receptors, permitting analysis of glutamate receptor responses in Xenopus oocytes. In combination with a crystallographic analysis of the GluRIIB ligand binding domain, we use this system to characterize the subunit dependence of assembly, channel block, and ligand selectivity for Drosophila NMJ glutamate receptors.