Format

Send to

Choose Destination
Biomol NMR Assign. 2017 Apr;11(1):117-121. doi: 10.1007/s12104-017-9733-z. Epub 2017 Feb 26.

1H, 13C and 15N backbone chemical shift assignments of camelid single-domain antibodies against active state µ-opioid receptor.

Author information

1
Institut de Genomique Fonctionnelle (IGF), CNRS, INSERM, Univ. Montpellier, F-34094, Montpellier, France. remy.sounier@igf.cnrs.fr.
2
Centre de Biochimie Structurale, CNRS UMR 5048-INSERM 1054, University of Montpellier, 29 rue de Navacelles, 34090, Montpellier Cedex, France.
3
Institut de Genomique Fonctionnelle (IGF), CNRS, INSERM, Univ. Montpellier, F-34094, Montpellier, France.
4
Centre de Biochimie Structurale, CNRS UMR 5048-INSERM 1054, University of Montpellier, 29 rue de Navacelles, 34090, Montpellier Cedex, France. helene.demene@cbs.cnrs.fr.

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.

KEYWORDS:

Camelid antibody; G protein coupled receptor; Nanobody

PMID:
28239762
PMCID:
PMC5406611
DOI:
10.1007/s12104-017-9733-z
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Springer Icon for PubMed Central
Loading ...
Support Center