G-protein coupled receptors (GPCR) comprise the largest family of cell-surface receptors, and their important role in physiology makes them the frequent target of therapeutic drugs. Due to a number of challenges involved in producing diffraction quality crystals of GPCR, the structural characterization of these molecules has been slow. The Parrill lab has been working on a strategy of introducing a transferable set of mutations that will render GPCR water-soluble with the aim of accelerating their structural characterization. Thus far, collecting data on the structure and function of the water soluble mutants has proved difficult, presumably due to lack of thermostability. This poster presents preliminary efforts to introduce previously published thermostability mutations into water soluble constructs of the human β2 adrenergic receptor (hβ2AR). Trial expressions of the thermostabilized mutants showed that they expressed at approximately equivalent levels to the original water soluble construct.

Thermostabilization of water soluble variants of the human β2 adrenergic receptor

249th National Meeting (2015)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.