The figure shows the crystal structure of a form of cytochrome P450 (CYP), CYP1A2², a form closely related to CYP1B1, an uncrystallized form of Family 1 CYP, with which it has been aligned to reveal structural impact of mutations¹. The yellowed residue labelled Cys is cysteine, which forms the 5^th heme ligand of the heme, and other yellow residues represent some of the mutation sites in CYP1B1causing primary congenital glaucoma. White letters on the cylinders indicate a-helices of CYP1A2².

1.         Choudhary D, Jansson I, Sarfarazi M, Schenkman JB: Characterization of the biochemical and structural phenotypes of four CYP1B1 mutations observed in individuals with primary congenital glaucoma. Pharmacogenet Genomics 2008;18:665-676.

2.         Sansen S, Yano JK, Reynald RL, Schoch GA, Griffin KJ, Stout CD, Johnson EF: Adaptations for the oxidation of polycyclic aromatic hydrocarbons exhibited by the structure of human P450 1A2. Journal of Biological Chemistry 2007;282:14348-14355.