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Structures of New Class of Protein Solved With the Help of Nano-Liquid Handling Technology

Major protein structure discovery achieved using TTP Labtech’s mosquito LCP

TTP LabTech LogoFor the first time, researchers have been able to successfully report the structure of a Class B G-Protein Coupled Receptor (GPCR) using lipidic cubic phase (LCP) protein crystallisation. The work performed at Heptares, a leading drug discovery and development company, and published this week in Nature, details the structural identification of the stress receptor, corticotropin-releasing factor receptor 1 (CRF1). This pioneering discovery opens up the technique to an entirely new group of molecules with important roles in the development of diseases as diverse as diabetes, osteoporosis, depression and anxiety. The mosquito LCP, an innovative solution for LCP crystallography designed by TTP Labtech, was a significant technical driving force enabling the research and underlines the company’s role in facilitating cutting-edge drug discovery research.

GPCRs are valuable drug targets

GPCRs are a family of proteins that play an essential part in cell signalling and are thus important drug targets for modulating cell function and influencing disease outcome. The Class B subset of GPCRs includes many peptide hormone receptors relevant for treating disease, such as glucagon, glucagon-like peptide, calcitonin and parathyroid peptide hormone. However, until the recent work carried out by Heptares, it had proven almost impossible to provide structural data for this class, severely hampering drug development efforts across the industry.

The finding that the structure of CRF1, a Class B GPCR, contains a novel binding pocket for the small molecule antagonist, towards the intracellular side of the receptor and far from the position of other Class A GPCR ligands, underlines the importance of the discovery; particularly in terms of modelling other Class B receptors and potentially unlocking drug design across the subset.


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