Access the full text.
Sign up today, get DeepDyve free for 14 days.
I Audenhove, J Gettemans (2016)
Nanobodies as versatile tools to understand, diagnose, visualize and treat cancerEBioMedicine, 8
E Genst (2006)
Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodiesProc Natl Acad Sci U S A, 103
WF Vranken (2005)
The CCPN data model for NMR spectroscopy: development of a software pipelineProteins, 59
X Deupi, BK Kobilka (2010)
Energy landscapes as a tool to integrate GPCR structure, dynamics, and functionPhysiology, 25
R Sounier (2015)
Propagation of conformational changes during mu-opioid receptor activationNature, 524
JL Pons, TE Malliavin, MA Delsuc (1996)
Gifa V. 4: a complete package for NMR data set processingJ Biomol NMR, 8
Y Shen, A Bax (2013)
Protein backbone and sidechain torsion angles predicted from NMR chemical shifts using artificial neural networksJ Biomol NMR, 56
W Huang (2015)
Structural insights into micro-opioid receptor activationNature, 524
JL Markley (1998)
Recommendations for the presentation of NMR structures of proteins and nucleic acids–IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopyEur J Biochem, 256
I Melnikova (2010)
Pain marketNat Rev Drug Discov, 9
F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer, A Bax (1995)
NMRPipe: a multidimensional spectral processing system based on UNIX pipesJ Biomol NMR, 6
DS Wishart (1995)
1 H, 13 C and 15 N chemical shift referencing in biomolecular NMRJ Biomol NMR, 6
C Hamers-Casterman (1993)
Naturally-occurring antibodies devoid of light-chainsNature, 363
CL Neilan (2004)
Characterization of the complex morphinan derivative BU72 as a high efficacy, long-lasting mu-opioid receptor agonistEur J Pharmacol, 499
V Salema, LA Fernandez (2013)
High yield purification of nanobodies from the periplasm of E. coli as fusions with the maltose binding proteinProtein Expr Purif, 91
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.
Biomolecular NMR Assignments – Springer Journals
Published: Feb 26, 2017
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.