title: NMR-based structural characterization of large protein-ligand interactions.
abstract: 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.
authors.affiliation: Triad Therapeutics, Inc., San Diego 92121, USA. mpellecchia@triadt.com
authors.forename: Maurizio
authors.initials: M
authors.lastname: Pellecchia
authors.forename: David
authors.initials: D
authors.lastname: Meininger
authors.forename: Qing
authors.initials: Q
authors.lastname: Dong
authors.forename: Edcon
authors.initials: E
authors.lastname: Chang
authors.forename: Rick
authors.initials: R
authors.lastname: Jack
authors.forename: Daniel S
authors.initials: DS
authors.lastname: Sem
mesh_terms: 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*
chemical_list: D008024:Ligands; D011506:Proteins