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Stabilizing, camelid-derived nanobodies to facilitate generation of crystal structures of GPCRs bound to low-affinity, natural ligands

Stabilizing, camelid-derived antibody fragments called nanobodies could be useful for generating the crystal structure of GPCRs bound to low-affinity, natural ligands. A camelid nanobody with high affinity for the activated form of adrenergic receptor b2 (ADRB2) was used to stabilize the receptor. This enabled the crystallization and resolution of the receptor's structure in complex with three chemically distinct ligands, including the low-affinity ligand adrenaline. The receptor conformation was similar for all ligands. Next steps could include applying the approach to other therapeutically relevant GPCR and low-affinity ligand pairs.
Ablynx N.V., who was not involved in the current study, has multiple nanobodies in clinical and preclinical development for various diseases.

SciBX 6(40); doi:10.1038/scibx.2013.1145
Published online Oct. 17, 2013

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Ring, A.M. et al. Nature; published online Sept. 22, 2013;
Contact: Brian K. Kobilka, Stanford University, Stanford, Calif.
Contact: Christopher Garcia, same affiliation as above