NMR-based structural characterization of large protein-ligand interactions.
Genomic research on target identification and validation has created a great need for methods that rapidly provide detailed structural information on protein-ligand interactions. We developed a suite of NMR experiments as rapid and efficient tools to provide descriptive structural information on protein-ligand complexes. The methods work with large proteins and in particular cases also without the need for a complete three-dimensional structure. We will show applications with two tetrameric enzymes of 120 and 170 kDa.
Pellecchia
Maurizio
M
Triad Therapeutics, Inc., San Diego 92121, USA. mpellecchia@triadt.com
Meininger
David
D
Dong
Qing
Q
Chang
Edcon
E
Jack
Rick
R
Sem
Daniel S
DS
D001665:Binding Sites; D020650:Combinatorial Chemistry Techniques; D015195:Drug Design; D008024:Ligands; D008958:Models, Molecular; D015394:Molecular Structure; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000037:antagonists & inhibitors / Q000737:chemistry*
D008024:Ligands; D011506:Proteins