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NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions
[Image: see text] In order to examine the origins of the large positive cooperativity (ΔG(0)(coop) = −2.9 kcal mol(−1)) of trimethoprim (TMP) binding to a bacterial dihydrofolate reductase (DHFR) in the presence of NADPH, we have determined and compared NMR solution structures of L. casei apo DHFR a...
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| Main Authors: | , , , , , |
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| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
American Chemical Society
2011
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| Acesso em linha: | https://ncbi.nlm.nih.gov/pmc/articles/PMC3086361/ https://ncbi.nlm.nih.gov/pubmed/21410224 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi200067t |
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