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I study the structure and function of adhesion GPCRs using engineered protein probes.

In just the last decade the field of adhesion G protein-coupled receptor (aGPCR) biology has emerged as disease-relevant and biochemically fascinating. Whereas canonical GPCRs have short extracellular N-termini, aGPCRs have elongated and diverse N-termini, ranging from several hundred to over five thousand amino acids. I have engineered synthetic proteins based on a fibronectin III scaffold (termed monobodies) which bind with high affinity and specificity to a particular extracellular domain conserved between aGPCRs. I plan to use these and other monobodies to probe the N-terminal domains of aGPCRs in an effort to shed light on their physiological and pathophysiological roles.