NMR-Based Strategies to Elucidate Bioactive Conformations of Weakly Binding Ligands.
Topics in Current Chemistry-Series(2008)
摘要
Key processes in molecular biology are regulated by interactions between biomolecules. Protein-protein and protein-ligand interactions, e.g., in signal transduction pathways, rely on the subtle interactions between atoms at the binding interface of the involved molecules. Because biomolecules often have many interacting partners, these interactions are not necessarily strong. The study of molecular recognition gives insight into the complex network of signaling in life and is the basis of structure-based drug design. In the situation where the interaction is weak, one of the traditional methods that can be applied to obtain structural information (internuclear distances) of the bound ligand is the so-called transferred NOE (trNOE) method. Recently, it became possible to use transferred cross-correlated relaxation (trCCR) to directly measure dihedral angles. The combined use of these two techniques significantly improves the precision of the structure determination of ligands weakly bound to macromolecules. The application of these techniques will be discussed in detail for a peptide derived from IKK beta bound to the protein NEMO that plays an important role in the NF kappa B pathway.
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关键词
cross-correlated relaxation,IKK beta,NEMO,NMR,trCCR,trNOE
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