Structures of highly flexible intracellular domain of human α7 nicotinic acetylcholine receptor

Vasyl Bondarenko, Marta M. Wells, Qiang Chen, Tommy S. Tillman, Kevin Singewald, Matthew J. Lawless, Joel Caporoso, Nicole Brandon, Jonathan A. Coleman, Sunil Saxena, Erik Lindahl, Yan Xu and Pei Tang ()
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Vasyl Bondarenko: University of Pittsburgh
Marta M. Wells: University of Pittsburgh
Qiang Chen: University of Pittsburgh
Tommy S. Tillman: University of Pittsburgh
Kevin Singewald: University of Pittsburgh
Matthew J. Lawless: University of Pittsburgh
Joel Caporoso: University of Pittsburgh
Nicole Brandon: University of Pittsburgh
Jonathan A. Coleman: University of Pittsburgh
Sunil Saxena: University of Pittsburgh
Erik Lindahl: Stockholm University
Yan Xu: University of Pittsburgh
Pei Tang: University of Pittsburgh

Nature Communications, 2022, vol. 13, issue 1, 1-9

Abstract: Abstract 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 α7 nicotinic acetylcholine receptor in a resting state. We show that ~57% of the ICD residues are in highly flexible regions, primarily in a large loop (loop L) with the most mobile segment spanning ~50 Å 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.

Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28400-x

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DOI: 10.1038/s41467-022-28400-x

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