A detailed molecular model for human aromatase.
Using a variety of techniques, including sequence alignment, secondary structure prediction, molecular mechanics and molecular dynamics, we have constructed a model for the three-dimensional structure of P-450arom (human aromatase) based on that of P-450cam, the only cytochrome P-450 enzyme for which the crystal structure is known. The predicted structure is found to be in good agreement with current experimental data; both direct, from site-directed mutagenesis studies, and indirect, from the consideration of the structures and activities of known substrates and inhibitors.
Laughton
C A
CA
CRC Biomolecular Structure Unit, Institute of Cancer Research, Sutton, Surrey, England.
Zvelebil
M J
MJ
Neidle
S
S
D000595:Amino Acid Sequence; D001141:Aromatase / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D019475:Camphor 5-Monooxygenase; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D006899:Mixed Function Oxygenases / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012984:Software
D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D001141:Aromatase; D019475:Camphor 5-Monooxygenase