4H8I

Structure of GluK2-LBD in complex with GluAzo

Summary for 4H8I

• Entry DOI: 10.2210/pdb4h8i/pdb
• Related: 4H8J
• Descriptor: Glutamate receptor, ionotropic kainate 2, (4R)-4-[(2E)-3-{4-[(E)-phenyldiazenyl]phenyl}prop-2-en-1-yl]-L-glutamic acid, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: membrane protein, glycoprotein, transmembrane protein, ligand-binding domain, ion transport, ion channel, ionotropic glutamate receptor, kainate receptor, gluazo, pcl, photochromic ligand, mes, synapse, presynaptic cell membrane, postsynaptic cell membrane, signaling protein
• Biological source: Rattus norvegicus (rat); More
• Cellular location: Cell membrane ; Multi-pass membrane protein : P42260
• Total number of polymer chains: 2
• Total formula weight: 59437.42

Authors

Reiter, A.,Skerra, A.,Trauner, D.,Schiefner, A. (deposition date: 2012-09-22, release date: 2013-09-25, Last modification date: 2024-11-27)

Primary citation

Reiter, A.,Skerra, A.,Trauner, D.,Schiefner, A.
A photoswitchable neurotransmitter analogue bound to its receptor.
Biochemistry, 52:8972-8974, 2013

PubMed Abstract: Incorporation of the azobenzene derivative gluazo, a synthetic photochromic ligand, into a kainate receptor allows for the optical control of neuronal activity. The crystal structure of gluazo bound to a dimeric GluK2 ligand-binding domain reveals one monomer in a closed conformation, occupied by gluazo, and the other in an open conformation, with a bound buffer molecule. The glutamate group of gluazo interacts like the natural glutamate ligand, while its trans-azobenzene moiety protrudes into a tunnel. This elongated cavity presumably cannot accommodate a cis-azobenzene, which explains the reversible activation of the receptor upon photoisomerization.

PubMed: 24295282
DOI: 10.1021/bi4014402

Experimental method

X-RAY DIFFRACTION (2 Å)