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.
Original language | English (US) |
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Pages (from-to) | 8972-8974 |
Number of pages | 3 |
Journal | Biochemistry |
Volume | 52 |
Issue number | 50 |
DOIs | |
State | Published - Dec 17 2013 |
ASJC Scopus subject areas
- Biochemistry