Extended Data Figure 4 : Strychnine binding to GlyRα3.

From: Crystal structure of human glycine receptor-α3 bound to antagonist strychnine

Extended Data Figure 4

a, b, Two views of the strychnine-binding pocket showing 2FoFc omit electron density maps. The principal subunit is coloured pale green, the complementary subunit is cyan, and strychnine is grey. Strychnine was omitted from map calculations. Map is contoured at 1.0σ. The hydrogen bond between the backbone carbonyl of Phe159 and the tertiary nitrogen of strychnine is shown as a dotted line. c, d, Same views and representations as in a and b, but FoFc omit electron density is shown. Contour level of map is 3.0σ. e, Chemical structure of strychnine. Ring numbering is denoted by red Roman numerals. Carbon and nitrogen historic numbering conventions are denoted by blue numbers. f, Solvent-accessible surface area of the complementary side of the binding interface coloured by electrostatic potential. The complementary subunit interface has a positive electrostatic potential to interact with the partial negative charge of the lactam oxygen of strychnine.