Biochem Pharmacol. 1990 Jul 1;40(1):141-52.

NMR studies of interactions of ligands with dihydrofolate reductase.

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National Institute for Medical Research, Mill Hill, London, U.K.

Abstract

NMR spectroscopy is a useful technique for studying interactions, conformations and dynamic processes within ligand-protein complexes. Several examples of the application of the method to studies of complexes of anti-folate drugs with their target enzyme, dihydrofolate reductase, are discussed.

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NMR studies of differences in the conformations and dynamics of ligand complexes formed with mutant dihydrofolate reductases. [Biochemistry. 1989]
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Cited by 3 PubMed Central articles

Structure and dynamics in solution of the complex of Lactobacillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate. [Protein Sci. 1999]
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Correlation of trimethoprim and brodimoprim physicochemical and lipid membrane interaction properties with their accumulation in human neutrophils. [Antimicrob Agents Chemother. 1...]
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Fresta M, Furneri PM, Mezzasalma E, Nicolosi VM, Puglisi G. Antimicrob Agents Chemother. 1996 Dec; 40(12):2865-73.
3H-n.m.r. studies of multiple conformations and dynamic processes in complexes of folate and methotrexate with Lactobacillus casei dihydrofolate reductase. [Biochem J. 1994]
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Curtis N, Moore S, Birdsall B, Bloxsidge J, Gibson CL, Jones JR, Feeney J. Biochem J. 1994 Oct 15; 303 ( Pt 2):401-5.

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