Fig. 2: Overall structure of GABARAPL1 in complex with γ2-GIM and characterization of key residues at the interface of the GABARAPL1–γ2-GIM complex. | Nature Communications

Fig. 2: Overall structure of GABARAPL1 in complex with γ2-GIM and characterization of key residues at the interface of the GABARAPL1–γ2-GIM complex.

From: Structural basis of GABARAP-mediated GABAA receptor trafficking and functions on GABAergic synaptic transmission

Fig. 2

a Ribbon representation model showing the overall structure of the GABARAPL1–γ2-GIM complex. In this drawing, GABARAPL1 is shown in forest green and γ2-GIM is in orange. The coordinates and structure factors of the GABARAP and γ2-GABAAR complex have been deposited in the Protein Data Bank with accession number 7CDB. b The Fo−Fc map of γ2-GIM showing that the densities of residues 402–413 can be clearly assigned. c Stereo view showing the detailed interactions between γ2-GIM and GABARAPL1. The hydrogen bonds involved in the binding are shown as dotted lines. d ITC-derived binding curves comparing the binding affinities between γ2-GIM and GABARAP or its six mutant variants (E17A, K24E, Y49A, L50A, K66E, and R67E). e ITC-derived binding curves comparing binding affinities between GABARAP and γ2-GIM or its five mutant variants (E402T, Y403E, Y405E, E406R, and L408Q).

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