Jiannan Wang, Xiaogang Niu, Changwen Jin, Yunfei Hu
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引用次数: 0
Abstract
G protein-coupled receptors (GPCRs) are highly dynamic seven-transmembrane (7TM) proteins that respond to various extracellular stimuli and elicit diverse intracellular signaling cascades. The third intracellular loops (ICL3s) of the GPCRs are intrinsically disordered and play important roles in signaling. The muscarinic acetylcholine receptors (mAChRs) harbor extremely long ICL3s, which comprise over a hundred amino acid residues and contain multiple phosphorylation sites. Due to their intrinsic flexibility, ICL3s are commonly absent or unobservable in cryo-EM or X-ray structures, and there has been a lack of structural and dynamics study of these regions. Herein, we report the 1H, 13C and 15N chemical shift assignments of the M1 muscarinic receptor ICL3, which provides a basis for further NMR studies of its conformational dynamics, post-translational modifications and interactions.
期刊介绍：
Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties.
Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
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