Abstract
Nanobodies are single chain antibodies that have become a highly valuable and versatile tool for biomolecular and therapeutic research. One application field is the stabilization of active states of flexible proteins, among which G-protein coupled receptors represent a very important class of membrane proteins. Here we present the backbone and side-chain assignment of the 1H, 13C and 15N resonances of Nb33 and Nb39, two nanobodies that recognize and stabilize the µ-opioid receptor to opioids in its active agonist-bound conformation. In addition, we present a comparison of their secondary structures as derived from NMR chemical shifts.
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Acknowledgements
This work used the NMR FRISBI (French Infrastructure for Integrated Structural Biology) platform in Montpellier, with support from the “Agence nationale de la recherche” of France, ANR-10-INSB-05-0 (YY and HD). We acknowledge the GIS “IBiSA: Infrastructures en Biologie Santé et Agronomie” and the support from the National Institutes of Health Grant (NIDA-DA036246 to SG).
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Sounier, R., Yang, Y., Hagelberger, J. et al. 1H, 13C and 15N backbone chemical shift assignments of camelid single-domain antibodies against active state µ-opioid receptor. Biomol NMR Assign 11, 117–121 (2017). https://doi.org/10.1007/s12104-017-9733-z
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DOI: https://doi.org/10.1007/s12104-017-9733-z