Hepatitis B virus (HBV) capsid assembly modulators (CAMs) represent a recent class of anti-HBV antivirals. CAMs disturb proper nucleocapsid assembly, by inducing formation of either aberrant assemblies (CAM-A) or of apparently normal but genome-less empty capsids (CAM-E). Classical structural approaches have revealed the CAM binding sites on the capsid protein (Cp), but conformational information on the CAM-induced off-path aberrant assemblies is lacking. Here we show that solid-state NMR can...
[NMR paper] Fast Magic-Angle-Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid*C-Terminal Domain
Fast Magic-Angle-Spinning NMR Reveals the Evasive Hepatitis B Virus Capsid*C-Terminal Domain
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...
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06-03-2022 07:40 PM
[NMR paper] Experimental Characterization of the Hepatitis B Virus Capsid Dynamics by Solid-State NMR
Experimental Characterization of the Hepatitis B Virus Capsid Dynamics by Solid-State NMR
Protein plasticity and dynamics are important aspects of their function. Here we use solid-state NMR to experimentally characterize the dynamics of the 3.5 MDa hepatitis B virus (HBV) capsid, assembled from 240 copies of the Cp149 core protein. We measure both T (1) and T (1?) relaxation times, which we use to establish detectors on the nanosecond and microsecond timescale. We compare our results to those from a 1 microsecond all-atom Molecular Dynamics (MD) simulation trajectory for the capsid....
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01-21-2022 10:06 AM
[NMR paper] Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.
Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.
Related Articles Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR.
J Biomol NMR. 2018 Jan 18;:
Authors: Gupta S, Tycko R
Abstract
Recent studies of noncrystalline HIV-1 capsid protein (CA) assemblies by our laboratory and by Polenova and coworkers (Protein Sci 19:716-730, 2010; J Mol Biol 426:1109-1127, 2014; J Biol Chem 291:13098-13112, 2016; J Am Chem Soc 138:8538-8546, 2016; J Am Chem Soc 138:12029-12032, 2016;...
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02-23-2018 03:44 AM
Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR
Segmental isotopic labeling of HIV-1 capsid protein assemblies for solid state NMR
Abstract
Recent studies of noncrystalline HIV-1 capsid protein (CA) assemblies by our laboratory and by Polenova and coworkers (Protein Sci 19:716â??730, 2010; J Mol Biol 426:1109â??1127, 2014; J Biol Chem 291:13098â??13112, 2016; J Am Chem Soc 138:8538â??8546, 2016; J Am Chem Soc 138:12029â??12032, 2016; J Am Chem Soc 134:6455â??6466, 2012; J Am Chem Soc 132:1976â??1987, 2010; J Am Chem Soc 135:17793â??17803, 2013; Proc Natl Acad Sci USA 112:14617â??14622, 2015; J Am...
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02-21-2018 12:45 AM
[NMR paper] Solid-state [13C-15N] NMR resonance assignment of hepatitis B virus core protein.
Solid-state NMR resonance assignment of hepatitis B virus core protein.
Related Articles Solid-state NMR resonance assignment of hepatitis B virus core protein.
Biomol NMR Assign. 2018 Feb 16;:
Authors: Lecoq L, Wang S, Wiegand T, Bressanelli S, Nassal M, Meier BH, Böckmann A
Abstract
Each year, nearly 900,000 deaths are due to serious liver diseases caused by chronic hepatitis B virus infection. The viral particle is composed of an outer envelope and an inner icosahedral nucleocapsid formed by multiple dimers of a ~ 20*kDa...
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02-18-2018 05:54 AM
Structure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular Assemblies
Structure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular Assemblies
Marvin J. Bayro and Robert Tycko
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b03983/20160628/images/medium/ja-2016-03983c_0006.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b03983
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/yXorzqET3DQ
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06-29-2016 09:52 AM
[NMR paper] Structure of the dimerization interface in the mature HIV-1 capsid protein lattice from solid state NMR of tubular assemblies.
Structure of the dimerization interface in the mature HIV-1 capsid protein lattice from solid state NMR of tubular assemblies.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structure of the dimerization interface in the mature HIV-1 capsid protein lattice from solid state NMR of tubular assemblies.
J Am Chem Soc. 2016 Jun 14;
Authors: Bayro MJ, Tycko R
Abstract
The HIV-1 capsid protein (CA) forms the capsid shell that encloses RNA within a mature...
Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR
Linear Mode
