NMR spectroscopy and other techniques underpin research at the University of Southampton into how changes in the cell membrane play a pivotal role in how the Hepatitis C virus replicates.
Transverse relaxation dispersion of the p7 membrane channel from hepatitis C virus reveals conformational breathing
Transverse relaxation dispersion of the p7 membrane channel from hepatitis C virus reveals conformational breathing
Abstract
The p7 membrane protein encoded by hepatitis C virus (HCV) assembles into a homo-hexamer that selectively conducts cations. An earlier solution NMR structure of the hexameric complex revealed a funnel-like architecture and suggests that a ring of conserved asparagines near the narrow end of the funnel are important for cation interaction. NMR based drug-binding experiments also suggest that rimantadine can allosterically inhibit...
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02-27-2015 11:13 AM
[NMR paper] Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Related Articles Global fold and backbone dynamics of the hepatitis C virus E2 glycoprotein transmembrane domain determined by NMR.
Biochim Biophys Acta. 2014 Aug 7;
Authors: Shalom-Elazari H, Zazrin-Greenspon H, Shaked H, Chill JH
Abstract
E1 and E2 are two hepatitis C viral envelope glycoproteins that assemble into a heterodimer that is essential for membrane fusion and penetration into the target cell. Both...
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08-12-2014 06:25 PM
19F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus
19F NMR Reveals Multiple Conformations at the Dimer Interface of the Nonstructural Protein 1 Effector Domain from Influenza A Virus
Publication date: Available online 27 February 2014
Source:Structure</br>
Author(s): James*M. Aramini , Keith Hamilton , Li-Chung Ma , G.V.T. Swapna , Paul*G. Leonard , John*E. Ladbury , Robert*M. Krug , Gaetano*T. Montelione</br>
Nonstructural protein 1 of influenza A virus (NS1A) is a*conserved virulence factor comprised of an N-terminal double-stranded RNA (dsRNA)-binding domain and a multifunctional C-terminal effector domain...
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02-28-2014 06:08 AM
[NMR paper] Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.
Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.
Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.
Biochim Biophys Acta. 2013 Nov 2;
Authors: Zazrin H, Shaked H, Chill JH
Abstract
Oligomerization of hepatitis C viral envelope proteins E1 and E2 is essential to virus fusion and assembly. Although interactions within the transmembrane (TM) domains of these glycoproteins have proven contributions to the E1/E2 heterodimerization process and consequent...
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11-07-2013 11:06 AM
[NMR paper] Solution structure of mouse hepatitis virus (MHV) nsp3a and determinants of the interaction with MHV nucleocapsid (N) protein.
Solution structure of mouse hepatitis virus (MHV) nsp3a and determinants of the interaction with MHV nucleocapsid (N) protein.
Related Articles Solution structure of mouse hepatitis virus (MHV) nsp3a and determinants of the interaction with MHV nucleocapsid (N) protein.
J Virol. 2013 Jan 9;
Authors: Keane SC, Giedroc DP
Abstract
Coronaviruses (CoVs) are positive-sense, single-stranded, enveloped RNA viruses that infect a variety of vertebrate hosts. The CoV nucleocapsid (N) protein contains two structurally independent RNA binding domains...
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02-03-2013 10:22 AM
[NMR paper] The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--fr
The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--from the NMR tube to the clinic.
Related Articles The design of a potent inhibitor of the hepatitis C virus NS3 protease: BILN 2061--from the NMR tube to the clinic.
Biopolymers. 2004;76(4):309-23
Authors: Tsantrizos YS
The virally encoded serine protease NS3/NS4A is essential to the life cycle of the hepatitis C virus (HCV), an important human pathogen causing chronic hepatitis, cirrhosis of the liver, and hepatocellular carcinoma. Until very recently, the...
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11-24-2010 09:25 PM
[NMR paper] Hepatitis C virus NS3 protease requires its NS4A cofactor peptide for optimal binding
Hepatitis C virus NS3 protease requires its NS4A cofactor peptide for optimal binding of a boronic acid inhibitor as shown by NMR.
Related Articles Hepatitis C virus NS3 protease requires its NS4A cofactor peptide for optimal binding of a boronic acid inhibitor as shown by NMR.
Chem Biol. 2002 Jan;9(1):79-92
Authors: Archer SJ, Camac DM, Wu ZJ, Farrow NA, Domaille PJ, Wasserman ZR, Bukhtiyarova M, Rizzo C, Jagannathan S, Mersinger LJ, Kettner CA
NMR spectroscopy was used to characterize the hepatitis C virus (HCV) NS3 protease in a complex...
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11-24-2010 08:49 PM
NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
Related Articles NMR structure and ion channel activity of the p7 protein from hepatitis C virus.
J Biol Chem. 2010 Jul 28;
Authors: Montserret R, Saint N, Vanbelle C, Salvay AG, Simorre JP, Ebel C, Sapay N, Renisio JG, Bockmann A, Steinmann E, Pietschmann T, Dubuisson J, Chipot C, Penin F
The small membrane protein p7 of hepatitis C virus forms oligomers and exhibits ion channel activity essential for virus infectivity. These viroporin features render p7 an...
Hepatitis C Virus: NMR reveals replication essentials
NMR spectroscopy and other techniques underpin research at the University of Southampton into how changes in the cell membrane play a pivotal role in how the Hepatitis C virus replicates. 
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