By Carla Emery
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Feeney J (1990) NMR studies of interactions of ligands with dihydrofolate reductase. Biochemical Pharmacology 40: 141–152. Feeney J and Birdsall B (1993) NMR studies of protein–ligand interactions. NMR of Macromolecules 7: 183–215. Fesik SW (1993) NMR structure-based drug design. Journal of Biomolecular NMR 3: 261–269. Fesik SW, Gampe RT Jr, Holzman TF, et al (1990) Isotope-edited NMR of cyclosporin A bound to cyclophilin: evidence for a trans 9,10 amide bond. Science 250: 1406–1409. Handschumacher RE and Armitage IM (eds) (1990) NMR methods for elucidating macromolecule–ligand interactions: an approach to drug design.
Thus, individual protein interactions involving both the pyrimidine ring and the benzyl ring are involved in transient fluctuations during the lifetime of the complex (see Figure 1). If these structural fluctuations take place in close succession, they could form part of a sequence of events leading to complete dissociation of the complex. Future perspectives It is clear that advances in NMR methodology, particularly in multidimensional NMR experiments used in conjunction with isotopically labelled molecules, will provide even more detailed information about protein–ligand complexes in solution.
Jardetzky O and Roberts GCK (1981) NMR in Molecular Biology. London: Academic Press. Markley JL (1975) Observation of histidine residues in proteins by means of nuclear magnetic resonance spectroscopy. Accounts of Chemical Research 8: 70–80. Roberts GCK (ed), (1993) NMR of Macromolecules: A Practical Approach. New York: Oxford University Press. Shuker SB, Hajduk PJ, Meadows RP and Fesik SW (1996) Discovering high-affinity ligands for proteins – SAR by NMR. Science 274: 1531–1534. Watts A, Ulrich AS and Middleton DA (1995) Membrane protein structure: the contribution and potential of novel solid state NMR approaches.