Related ArticlesHelical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles.
J Am Chem Soc. 2016 Sep 21;138(37):12029-12032
Authors: Bayro MJ, Ganser-Pornillos BK, Zadrozny KK, Yeager M, Tycko R
Abstract
Maturation of HIV-1 requires disassembly of the Gag polyprotein lattice, which lines the viral membrane in the immature state, and subsequent assembly of the mature capsid protein lattice, which encloses viral RNA in the mature state. Metastability of the immature lattice has been proposed to depend on the existence of a structurally ordered, ?-helical segment spanning the junction between capsid (CA) and spacer peptide 1 (SP1) subunits of Gag, a segment that is dynamically disordered in the mature capsid lattice. We report solid state nuclear magnetic resonance (ssNMR) measurements on the immature lattice in noncrystalline, spherical virus-like particles (VLPs) derived from Gag. The ssNMR data provide definitive evidence for this critical ?-helical segment in the VLPs. Differences in ssNMR chemical shifts and signal intensities between immature and mature lattice assemblies also support a major rearrangement of intermolecular interactions in the maturation process, consistent with recent models from electron cryomicroscopy and X-ray crystallography.
PMID: 27593947 [PubMed - as supplied by publisher]
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
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http://feeds.feedburner.com/~r/acs/jacsat/~4/yXorzqET3DQ
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Solid-StateNMR Investigation of the Conformation,Proton Conduction, and Hydration of the Influenza B Virus M2 TransmembraneProton Channel
Solid-StateNMR Investigation of the Conformation,Proton Conduction, and Hydration of the Influenza B Virus M2 TransmembraneProton Channel
Jonathan K. Williams, Daniel Tietze, Myungwoon Lee, Jun Wang and Mei Hong
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/jacs.6b03142/20160623/images/medium/ja-2016-03142j_0010.gif
Journal of the American Chemical Society
DOI: 10.1021/jacs.6b03142
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06-24-2016 12:27 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...
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06-15-2016 11:12 PM
[NMR paper] Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel.
Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel.
Related Articles Solid-State NMR Investigation of the Conformation, Proton Conduction, and Hydration of the Influenza B Virus M2 Transmembrane Proton Channel.
J Am Chem Soc. 2016 Jun 10;
Authors: Williams JK, Tietze D, Lee M, Wang J, Hong M
Abstract
Together with the influenza A virus, influenza B virus causes seasonal flu epidemics. The M2 protein of influenza B (BM2) forms a tetrameric...
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06-11-2016 01:09 PM
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions
Abstract
The membrane proteins of viruses play critical roles in the virus life cycle and are attractive targets for therapeutic intervention. Virus-like particles (VLP) present the possibility to study the biochemical and biophysical properties of viral membrane proteins in their native environment. Specifically, the VLP constructs contain the entire protein sequence and are comprised of native membrane components including lipids, cholesterol,...
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02-29-2016 04:37 PM
[NMR paper] Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.
J Biomol NMR. 2016 Feb 26;
Authors: Antanasijevic A, Kingsley C, Basu A, Bowlin TL, Rong L, Caffrey M
Abstract
The membrane proteins of viruses play critical roles in the virus life cycle and are attractive targets for therapeutic intervention. Virus-like particles (VLP) present the possibility to study the biochemical...
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02-28-2016 03:10 PM
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Structure and dynamics of the lipid modifications of a transmembrane ?-helical peptide determined by (2)H solid-state NMR spectroscopy.
Biochim Biophys Acta. 2010 Dec 28;
Authors: Penk A, Müller M, Scheidt HA, Langosch D, Huster D
The fusion of biological membranes is mediated by integral membrane proteins with ?-helical transmembrane segments. Additionally, those proteins are often modified by the covalent...
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01-05-2011 09:51 PM
[NMR paper] Structure of the coat protein in fd filamentous bacteriophage particles determined by
Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.
Related Articles Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.
Proc Natl Acad Sci U S A. 2003 May 27;100(11):6458-63
Authors: Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ
The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined...
Helical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles.
Linear Mode
