Using the fragment molecular orbital method to investigate agonist-orexin-2 receptor interactions.

ABSTRACT: The understanding of binding interactions between any protein and a small molecule plays a key role in the rationalization of affinity and selectivity and is essential for an efficient structure-based drug discovery (SBDD) process. Clearly, to begin SBDD, a structure is needed, and although there has been fantastic progress in solving G-protein-coupled receptor (GPCR) crystal structures, the process remains quite slow and is not currently feasible for every GPCR or GPCR-ligand complex. This situation significantly limits the ability of X-ray crystallography to impact the drug discovery process for GPCR targets in 'real-time' and hence there is still a need for other practical and cost-efficient alternatives. We present here an approach that integrates our previously described hierarchical

SUBMITTER: Heifetz A 

PROVIDER: S-EPMC5264495 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature