Sounier Remy, Yang Yinshan, Hagelberger Joanna, Granier Sébastien, Déméné Hélène
Institut de Genomique Fonctionnelle (IGF), CNRS, INSERM, Univ. Montpellier, F-34094, Montpellier, France.
Centre de Biochimie Structurale, CNRS UMR 5048-INSERM 1054, University of Montpellier, 29 rue de Navacelles, 34090, Montpellier Cedex, France.
Biomol NMR Assign. 2017 Apr;11(1):117-121. doi: 10.1007/s12104-017-9733-z. Epub 2017 Feb 26.
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 H, C and N 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.
纳米抗体是单链抗体,已成为生物分子和治疗研究中极具价值且用途广泛的工具。一个应用领域是稳定柔性蛋白质的活性状态,其中G蛋白偶联受体是一类非常重要的膜蛋白。在此,我们展示了Nb33和Nb39这两种纳米抗体的H、C和N共振的主链和侧链归属,这两种纳米抗体可识别并稳定处于活性激动剂结合构象的μ-阿片受体与阿片类物质的结合。此外,我们还比较了由NMR化学位移推导得出的它们的二级结构。