A detailed molecular model for human aromatase
作者： C.A. Laughton , M.J.J.M. Zvelbil , S. Neidle
DOI: 10.1016/0960-0760(93)90243-P
关键词:
摘要: Using a variety of techniques, including sequence alignment, secondary structure prediction, molecular mechanics and dynamics, we have constructed model for the three-dimensional P-450arom (human aromatase) based on that P-450cam, only cytochrome P-450 enzyme which crystal is known. The predicted found to be in good agreement with current experimental data; both direct, from site-directed mutagenesis studies, indirect, consideration structures activities known substrates inhibitors.
sci-hub.se 参考文章(34)
Christos A. OUZOUNIS, William T. MELVIN, Primary and secondary structural patterns in eukaryotic cytochrome P-450 families correspond to structures of the helix-rich domain of Pseudomonas putida cytochrome P-450cam. Indications for a similar overall topology. FEBS Journal. ,vol. 198, pp. 307- 315 ,(1991) , 10.1111/J.1432-1033.1991.TB16017.X
Neena L. Summers, Martin Karplus, Construction of side-chains in homology modelling. Application to the C-terminal lobe of rhizopuspepsin. Journal of Molecular Biology. ,vol. 210, pp. 785- 811 ,(1989) , 10.1016/0022-2836(89)90109-5
Geoffrey J. Barton, Michael J.E. Sternberg, A strategy for the rapid multiple alignment of protein sequences. Confidence levels from tertiary structure comparisons. Journal of Molecular Biology. ,vol. 198, pp. 327- 337 ,(1987) , 10.1016/0022-2836(87)90316-0
D J Zhou, K R Korzekwa, T Poulos, S A Chen, A site-directed mutagenesis study of human placental aromatase. Journal of Biological Chemistry. ,vol. 267, pp. 762- 768 ,(1992) , 10.1016/S0021-9258(18)48349-4
M J McPhaul, J F Noble, E R Simpson, C R Mendelson, J D Wilson, The expression of a functional cDNA encoding the chicken cytochrome P-450arom (aromatase) that catalyzes the formation of estrogen from androgen. Journal of Biological Chemistry. ,vol. 263, pp. 16358- 16363 ,(1988) , 10.1016/S0021-9258(18)37601-4
J.T. Kellis, W.E. Childers, C.H. Robinson, L.E. Vickery, Inhibition of aromatase cytochrome P-450 by 10-oxirane and 10-thiirane substituted androgens: implications for the structure of the active site Journal of Biological Chemistry. ,vol. 262, pp. 4421- 4426 ,(1987) , 10.1016/S0021-9258(18)61365-1
S. Graham-Lorence, M.W. Khalil, M.C. Lorence, C.R. Mendelson, E.R. Simpson, Structure-function relationships of human aromatase cytochrome P-450 using molecular modeling and site-directed mutagenesis. Journal of Biological Chemistry. ,vol. 266, pp. 11939- 11946 ,(1991) , 10.1016/S0021-9258(18)99048-4
Jean P. Van Wauwe, Paul A. J. Janssen, Is there a case for P-450 inhibitors in cancer treatment? Journal of Medicinal Chemistry. ,vol. 32, pp. 2231- 2239 ,(1989) , 10.1021/JM00130A001
Markéta J.J.M. Zvelebil, C.Roland Wolf, Michael J.E. Sternberg, A predicted three-dimensional structure of human cytochrome P450: implications for substrate specificity "Protein Engineering, Design and Selection". ,vol. 4, pp. 271- 282 ,(1991) , 10.1093/PROTEIN/4.3.271
D. J. Zhou, D. Pompon, S. A. Chen, Structure-function studies of human aromatase by site-directed mutagenesis: kinetic properties of mutants Pro-308----Phe, Tyr-361----Phe, Tyr-361----Leu, and Phe-406----Arg. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 88, pp. 410- 414 ,(1991) , 10.1073/PNAS.88.2.410