The structural effects nanobodies towards Gai
Presentation Type
Poster
Faculty Mentor’s Full Name
Levi McClelland
Faculty Mentor’s Department
Division of biological sciences
Abstract / Artist's Statement
G protein coupled receptors (GPCRs) are responsible for converting extracellular messenger signals (ligands) to activation of metabolic pathways intracellularly. These signals are transduced using guanine nucleotide binding proteins (G proteins) that exchange GDP for GTP. G proteins are heterotrimers consisting of alpha (𝜶), beta (β), and gamma (γ) subunits. We have designed two nanobodies (NB), or antibody fragments, with high affinity for the G𝜶i subunit. Our research features two such nanobodies; NB9155 and NB9156, with the goal of understanding how G𝜶i:NB complex formation will affect protein stability and structure. As NB9155 and NB9156 have different binding sites for G𝜶i, we also investigate nanobody effects on guanine nucleotide exchange rates and potential chaperone activity. Our data will include confirmation of molecular weights using the Multi-Angle Light Scattering technique, monitoring nucleotide exchange rates using a Fluorescence Spectrometer, and comparison of crystal structures, determined by X-ray diffraction, for the G𝜶i:NB9155 and the G𝜶i:NB9156 crystal structures.
Category
Life Sciences
The structural effects nanobodies towards Gai
UC South Ballroom
G protein coupled receptors (GPCRs) are responsible for converting extracellular messenger signals (ligands) to activation of metabolic pathways intracellularly. These signals are transduced using guanine nucleotide binding proteins (G proteins) that exchange GDP for GTP. G proteins are heterotrimers consisting of alpha (𝜶), beta (β), and gamma (γ) subunits. We have designed two nanobodies (NB), or antibody fragments, with high affinity for the G𝜶i subunit. Our research features two such nanobodies; NB9155 and NB9156, with the goal of understanding how G𝜶i:NB complex formation will affect protein stability and structure. As NB9155 and NB9156 have different binding sites for G𝜶i, we also investigate nanobody effects on guanine nucleotide exchange rates and potential chaperone activity. Our data will include confirmation of molecular weights using the Multi-Angle Light Scattering technique, monitoring nucleotide exchange rates using a Fluorescence Spectrometer, and comparison of crystal structures, determined by X-ray diffraction, for the G𝜶i:NB9155 and the G𝜶i:NB9156 crystal structures.