Anatomical Neuropharmacology Unit

This is an historical archive of the activities of the MRC Anatomical Neuropharmacology Unit (MRC ANU) that operated at the University of Oxford from 1985 until March 2015. The MRC ANU established a reputation for world-leading research on the brain, for training new generations of scientists, and for engaging the general public in neuroscience. The successes of the MRC ANU are now built upon at the MRC Brain Network Dynamics Unit at the University of Oxford.

Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.

J. Mol. Biol. 2009;392(5):1125-32. 10.1016/j.jmb.2009.07.082

Crystal structure of the GluR2 amino-terminal domain provides insights into the architecture and assembly of ionotropic glutamate receptors.

Clayton A, Siebold C, Gilbert RJC, Sutton GC, Harlos K, McIlhinney RAJ, Jones YE, Aricescu RA

Full text PDF download:

clayton2009jmolbiol.pdf

Abstract:

Ionotropic glutamate receptors are functionally diverse but have a common architecture, including the 400-residue amino-terminal domain (ATD). We report a 1.8-A resolution crystal structure of human GluR2-ATD. This dimeric structure provides a mechanism for how the ATDs can drive receptor assembly and subtype-restricted composition. Lattice contacts in a 4.1-A resolution crystal form reveal a tetrameric (dimer-dimer) arrangement consistent with previous cellular and cryo-electron microscopic data for full-length AMPA receptors.

Research and Techniques:

Crystallography, X-Ray

Models, Molecular

Protein Multimerization

Protein Structure, Quaternary

Protein Structure, Tertiary

Receptors, AMPA