Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 61, Issue 32, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202201083
Keywords
Viral Capsid; Dynamics; Hepatitis B Virus; Relaxation; Solid-State NMR
Categories
Funding
- ERC Advanced Grant [741863]
- Swiss National Science Foundation [200020_ 159707, 200020_188711]
- French ANRS [ECTZ71388, ECTZ100488]
- CNRS (CNRSMomentum 2018)
- Eidgenossische Technische Hochschule Zurich
- European Research Council (ERC) [741863] Funding Source: European Research Council (ERC)
- Swiss National Science Foundation (SNF) [200020_159707, 200020_188711] Funding Source: Swiss National Science Foundation (SNF)
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This study reports a new solid-state NMR technique that allows for the detection and characterization of the C-terminal domain of the hepatitis B virus capsid protein. It extends the capabilities of solid-state NMR and can provide insights into other flexible protein domains.
Experimentally determined protein structures often feature missing domains. One example is the C-terminal domain (CTD) of the hepatitis B virus capsid protein, a functionally central part of this assembly, crucial in regulating nucleic-acid interactions, cellular trafficking, nuclear import, particle assembly and maturation. However, its structure remained elusive to all current techniques, including NMR. Here we show that the recently developed proton-detected fast magic-angle-spinning solid-state NMR at >100 kHz MAS allows one to detect this domain and unveil its structural and dynamic behavior. We describe the experimental framework used and compare the domain's behavior in different capsid states. The developed approaches extend solid-state NMR observations to residues characterized by large-amplitude motion on the microsecond timescale, and shall allow one to shed light on other flexible protein domains still lacking their structural and dynamic characterization.
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