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Structures of highly flexible intracellular domain of human alpha 7 nicotinic acetylcholine receptor
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- Bondarenko, Vasyl (author)
- Univ Pittsburgh, Dept Anesthesiol & Perioperat Med, Pittsburgh, PA 15260 USA.
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- Wells, Marta M. (author)
- Univ Pittsburgh, Dept Anesthesiol & Perioperat Med, Pittsburgh, PA 15260 USA.
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- Chen, Qiang (author)
- Univ Pittsburgh, Dept Anesthesiol & Perioperat Med, Pittsburgh, PA 15260 USA.
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- Univ Pittsburgh, Dept Anesthesiol & Perioperat Med, Pittsburgh, PA 15260 USA Univ Pittsburgh, Dept Chem, Pittsburgh, PA 15260 USA. (creator_code:org_t)
- 2022-02-10
- 2022
- English.
- In: Nature Communications. - : Springer Nature. - 2041-1723. ; 13:1
- Journal article (peer-reviewed)
Abstract
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- The intracellular domain (ICD) of Cys-loop receptors mediates diverse functions. To date, no structure of a full-length ICD is available due to challenges stemming from its dynamic nature. Here, combining nuclear magnetic resonance (NMR) and electron spin resonance experiments with Rosetta computations, we determine full-length ICD structures of the human alpha 7 nicotinic acetylcholine receptor in a resting state. We show that similar to 57% of the ICD residues are in highly flexible regions, primarily in a large loop (loop L) with the most mobile segment spanning similar to 50 angstrom from the central channel axis. Loop L is anchored onto the MA helix and virtually forms two smaller loops, thereby increasing its stability. Previously known motifs for cytoplasmic binding, regulation, and signaling are found in both the helices and disordered flexible regions, supporting the essential role of the ICD conformational plasticity in orchestrating a broad range of biological processes.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Cell- och molekylärbiologi (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Cell and Molecular Biology (hsv//eng)
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