Fig. 2

Evaluation of the secondary structure prediction of the L425H variant by molecular modelling. 2A: schematic structures of the original (left) and the mutant (right) amino acid. The backbone, which is the same for each amino acid, is coloured in red. The side chain, unique for each amino acid, is coloured in black. 2B: Overview of the protein in ribbon-presentation. The protein is coloured by element; α-helix = blue, β-strand = red, turn = green, 3/10 helix = yellow and random coil = cyan. Other molecules in the complex are coloured in grey when present. 2C: Overview of the protein in ribbon-presentation. The protein is coloured in grey, the side chain of the mutated residue is coloured in magenta and shown as small balls. The mutated residue is located in the cytoplasmic loop between the transmembrane helices TM4 and TM5. 2D Close-up of the mutation seen from three slightly different angles. The protein is coloured in grey, the side chains of both the wild-type and the mutant residue are shown and coloured in green and red respectively. The mutant differs in size and hydrophobic properties