Figure 2.

In silico protein modelling of CYP11B2 p.(Gly134Arg)

Crystal structure model 4DVQ of human aldosterone synthase (CYP11B2) in complex with deoxycorticosterone (13) was used to study interatomic interactions upon mutation, employing PyMOL. Positively charged amino acids are blue, negatively charged amino acids are red. p.(Gly134Arg) substitution (panels A and B, the affected amino acid is given in green) did not result in steric clashes or changes to hydrogen bridges (yellow dashed lines). However, dihedral angles of p.(Gly134Arg) are considerably different to wild-type; the arginine sidechain (black circle, panel D) is pointed outwards, so that the otherwise smooth patch of protein surface has a positively charged appendicle (panels C and D). This may influence protein-substrate dynamics, since it is in close proximity to a putative steroid product egress route (13)