Figure 3: X-ray crystal structure of GephE in complex with the GABAAR α3 peptide fragment. | Nature Communications

Figure 3: X-ray crystal structure of GephE in complex with the GABAAR α3 peptide fragment.

From: Molecular basis of the alternative recruitment of GABAA versus glycine receptors through gephyrin

Figure 3

(a) Cartoon representation of GephE in complex with the GABAAR α3-derived peptide α11WT (PDB-ID: 4TK1) colour-coded according to its subdomain architecture as indicated (scheme at the bottom). The residues of α11WT resolved in the structure (368FNIVGTTYP376) are shown as a stick model in orange. (b) Close-up view into the binding pocket. Surface representation of the GephE-binding pocket coloured according to a. The GABAAR peptide is tightly packed into the cleft formed by subdomains III and IV from one monomer, as well as subdomain IV′ from the other monomer. (c) FoFc omit electron density map of the GABAAR α3 peptide (stereo representation) contoured at an rms deviation of 2.5 in blue with the modelled peptide in stick representation.

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