4WXJ

Drosophila muscle GluRIIB complex with glutamate

Summary for 4WXJ

• Entry DOI: 10.2210/pdb4wxj/pdb
• Descriptor: Glutamate receptor IIB,Glutamate receptor IIB, GLUTAMIC ACID (3 entities in total)
• Functional Keywords: glutamate receptor ion channel ligand binding domain, membrane protein
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 61986.90

Authors

Dharkar, P.,Mayer, M.L. (deposition date: 2014-11-13, release date: 2015-04-29, Last modification date: 2024-10-30)

Primary citation

Han, T.H.,Dharkar, P.,Mayer, M.L.,Serpe, M.
Functional reconstitution of Drosophila melanogaster NMJ glutamate receptors.
Proc.Natl.Acad.Sci.USA, 112:6182-6187, 2015

PubMed 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.

PubMed: 25918369
DOI: 10.1073/pnas.1500458112

Experimental method

X-RAY DIFFRACTION (2.002 Å)