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

被引：4

作者：

Sounier, Remy ^{[1
]}

Yang, Yinshan ^{[2
]}

Hagelberger, Joanna ^{[1
]}

Granier, Sebastien ^{[1
]}

Demene, Helene ^{[2
]}

机构：

[1] Univ Montpellier, CNRS, IGF, INSERM, F-34094 Montpellier, France

[2] Univ Montpellier, Ctr Biochim Struct, CNRS UMR 5048, INSERM 1054, 29 Rue Navacelles, F-34090 Montpellier, France

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2017年 / 11卷 / 01期

基金：

美国国家卫生研究院;

关键词：

Camelid antibody; Nanobody; G protein coupled receptor; NMR-SPECTROSCOPY; PROTEIN; ACTIVATION; NANOBODIES;

D O I：

10.1007/s12104-017-9733-z

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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-1, C-13 and N-15 resonances of Nb33 and Nb39, two nanobodies that recognize and stabilize the A mu-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.

引用

页码：117 / 121

页数：5

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