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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Detalles Bibliográficos
Autores principales: Feeney, James, Birdsall, Berry, Kovalevskaya, Nadezhda V., Smurnyy, Yegor. D., Navarro Peran, Emna M., Polshakov, Vladimir I.
Formato: Texto
Lenguaje:English
Publicado: American Chemical Society 2011
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086361/
https://www.ncbi.nlm.nih.gov/pubmed/21410224
http://dx.doi.org/10.1021/bi200067t

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