Novel mechanism-based substrates of dihydrofolate reductase and the thermodynamics of ligand binding: A comparison of theory and experiment for 8-methylpterin and 6,8-dimethylpterin
Author:
Publisher
Wiley
Subject
Molecular Biology,Biochemistry,Structural Biology
Reference55 articles.
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2. Crystal structure of human dihydrofolate reductase complexed with folate
3. Crystal structures of Escherichia coli dihydrofolate reductase: the NADP+ holoenzyme and the folate .cntdot. NADP+ ternary complex. substrate binding and a model for the transition state
4. Crystal structures of recombinant human dihydrofolate reductase complexed with folate and 5-deazafolate
5. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.
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3. Importance of Substrate and Cofactor Polarization in the Active Site of Dihydrofolate Reductase;Journal of Molecular Biology;2003-03
4. Combined Quantum and Molecular Mechanics (QM/MM) Study of the Ionization State of 8-Methylpterin Substrate Bound to Dihydrofolate Reductase;The Journal of Physical Chemistry B;2000-04-12
5. QM/MM and SCRF studies of the ionization state of 8-methylpterin substrate bound to dihydrofolate reductase: existence of a low-barrier hydrogen bond;Journal of Molecular Graphics and Modelling;2000-02
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