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Multiple sequence alignment of confirmed and predicted carbon-23 and carbon-24 CYP24A1 hydroxylases. (A) Semi-conservation of residues at positions 153, 164, and 170 of the C-D helices correlate with species predicted to have a regioselective preference for 1,25(OH)2D3 hydroxylation. Panel (B) demonstrates the locations of these residues in rat CYP24A1, in which all of the semi-conserved side chains are surface exposed and located near the Adx binding surface.
