A free-energy perturbation study of the binding of methotrexate to mutants of dihydrofolate reductase.
The importance of hydrophobic residues to the binding of methotrexate in the active site of dihydrofolate reductase (EC 1.5.1.3) was examined by a free-energy perturbation method. The replacement of a strictly conserved residue, Phe-31, by tyrosine or valine costs 1.8 and 5.1 kcal/mol, respectively,...
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| Pubblicato in: | Proc Natl Acad Sci U S A |
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| Autori principali: | , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
National Academy of Sciences
1988
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| Soggetti: | |
| Accesso online: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC282785/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/3200837/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.85.24.9519 |
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