Segment identification of a ligand binding with a protein receptor using multidimensional T1rho-, diffusion-filtered and diffusion-ordered NOESY experiments.
Multidimensional T1rho-, diffusion-filtered and diffusion-ordered NOESY techniques were applied to identify segments of a ligand binding with a protein receptor. These experiments can easily provide intermolecular NOEs of the complex, which are of great significance for characterizing the binding epitopes of a ligand. This information cannot be obtained by high-throughput 1D NMR experiments, used for determining the binding affinity, although multidimensional NMR experiments require more experiment time. The present results indicate that the current experiments using T1rho- and diffusion-edited techniques are very suitable for identifying segments of a ligand binding with a protein receptor in the drug discovery process.
NM Application & Research Group, Application & Research Center, Analytical Instruments Division, JEOL Ltd., Musashino, Akishima, Tokyo 196-8558, Japan.
Hiroaki
H
Utsumi
Hiroko
H
Seki
Kentaro
K
Yamaguchi
Mitsuru
M
Tashiro
D001665:Binding Sites; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry; D020156:Salicylic Acid / Q000737:chemistry*
D008024:Ligands; D011506:Proteins; D020156:Salicylic Acid