Related ArticlespH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.
Proc Natl Acad Sci U S A. 2012 Dec 4;109(49):19994-9
Authors: Lorieau JL, Louis JM, Schwieters CD, Bax A
Abstract
The highly conserved first 23 residues of the influenza hemagglutinin HA2 subunit constitute the fusion domain, which plays a pivotal role in fusing viral and host-cell membranes. At neutral pH, this peptide adopts a tight helical hairpin wedge structure, stabilized by aliphatic hydrogen bonding and charge-dipole interactions. We demonstrate that at low pH, where the fusion process is triggered, the native peptide transiently visits activated states that are very similar to those sampled by a G8A mutant. This mutant retains a small fraction of helical hairpin conformation, in rapid equilibrium with at least two open structures. The exchange rate between the closed and open conformations of the wild-type fusion peptide is ~40 kHz, with a total open-state population of ~20%. Transitions to these activated states are likely to play a crucial role in formation of the fusion pore, an essential structure required in the final stage of membrane fusion.
[NMR paper] Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
J Biomol NMR. 2013 Jan 18;
Authors: Ghosh U, Xie L, Weliky DP
Abstract...
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NMR Determination of Protein Partitioning into Membrane Domains with Different Curvatures and Application to the Influenza M2 Peptide
NMR Determination of Protein Partitioning into Membrane Domains with Different Curvatures and Application to the Influenza M2 Peptide
22 February 2012
Publication year: 2012
Source:Biophysical Journal, Volume 102, Issue 4</br>
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The M2 protein of the influenza A virus acts both as a drug-sensitive proton channel and mediates virus budding through membrane scission. The segment responsible for causing membrane curvature is an amphipathic helix in the cytoplasmic domain of the protein. Here, we use 31P and 13C solid-state NMR to examine M2-induced membrane curvature....
Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation
Whole-Body Rocking Motion of a Fusion Peptide in Lipid Bilayers from Size-Dispersed 15N NMR Relaxation
Justin L. Lorieau, John M. Louis and Ad Bax
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja2045309/aop/images/medium/ja-2011-045309_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja2045309
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/2aIqfWmdIn4
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Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Irregular structure of the HIV fusion peptide in membranes demonstrated by solid-state NMR and MD simulations.
Eur Biophys J. 2011 Jan 28;
Authors: Grasnick D, Sternberg U, Strandberg E, Wadhwani P, Ulrich AS
To better understand peptide-induced membrane fusion at a molecular level, we set out to determine the structure of the fusogenic peptide FP23 from the HIV-1 protein gp41 when bound to a lipid bilayer. An established solid-state...
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01-29-2011 12:35 PM
[NMR paper] An efficient fusion expression system for protein and peptide overexpression in Esche
An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Related Articles An efficient fusion expression system for protein and peptide overexpression in Escherichia coli and NMR sample preparation.
Protein Pept Lett. 2003 Apr;10(2):175-81
Authors: Cheng Y, Liu D, Feng Y, Jing G
An efficient fusion expression system with a small fusion partner, His6-tagged N-terminal fragment of staphylococcal nuclease R, has been constructed and tested with two genes. The results show that...
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Production of recombinant isotopically labelled peptide by fusion to an insoluble par
Production of recombinant isotopically labelled peptide by fusion to an insoluble partner protein: generation of integrin ?v?6 binding peptides for NMR.
Related Articles Production of recombinant isotopically labelled peptide by fusion to an insoluble partner protein: generation of integrin ?v?6 binding peptides for NMR.
Mol Biosyst. 2010 Oct 18;
Authors: Wagstaff JL, Howard MJ, Williamson RA
The integrin ?v?6 is up-regulated in several cancers and has clinical potential for both tumour imaging and therapy. Peptide ligands have been developed...
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10-19-2010 04:51 PM
[NMR paper] Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays
Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Analysis of a peptide inhibitor of paramyxovirus (NDV) fusion using biological assays, NMR, and molecular modeling.
Virology. 1997 Nov 24;238(2):291-304
Authors: Young JK, Hicks RP, Wright GE, Morrison TG
To investigate the molecular mechanisms involved in paramyxovirus-induced cell fusion, the function and...
pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR.
Linear Mode
