Structure-activity relationships for non-steroidal inhibitors of aromatase.
A model is described for the binding of non-steroidal inhibitors of aromatase to the enzyme with interaction of a ligand with the Fe3+-haem of the cytochrome. The model suggests that the inhibitors utilise a common binding site with ring A of the steroidal substrates.
Banting
L
L
Welsh School of Pharmacy, Cardiff, U.K.
Smith
H J
HJ
James
M
M
Jones
G
G
Nazareth
W
W
Nicholls
P J
PJ
Hewlins
M J
MJ
Rowlands
M G
MG
D000735:Androstenedione / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000494:pharmacology*; D047072:Aromatase Inhibitors; D001665:Binding Sites; D002786:Cholesterol Side-Chain Cleavage Enzyme / Q000037:antagonists & inhibitors; D003198:Computer Simulation; D005260:Female; D006801:Humans; D007700:Kinetics; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D010920:Placenta / Q000201:enzymology; D011247:Pregnancy; D013329:Structure-Activity Relationship
D047072:Aromatase Inhibitors; D000735:Androstenedione; D002786:Cholesterol Side-Chain Cleavage Enzyme