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针对活性态μ-阿片受体的骆驼科单域抗体的H、C和N主链化学位移归属

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

作者信息

Sounier Remy, Yang Yinshan, Hagelberger Joanna, Granier Sébastien, Déméné Hélène

机构信息

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.

出版信息

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

DOI:10.1007/s12104-017-9733-z
PMID:28239762
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5406611/
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 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.

摘要

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。