LEI 10882 DE 2004 PDF

Departamento de Física, Universidade de Aveiro, Aveiro, Portugal, CICECO, Universidade de Aveiro, Publication Date (Web): September 4, .. The Journal of Physical Chemistry C (29), .. Lei Zhang, Linlin Fu, Xingxing Yang, Zuoling Fu, Xiangdong Qi, Zhijian Wu. Chem., , (26), pp – Qian Zhou, Kendall Fitzgerald, Paul D. Boyle and Wesley A. Henderson Shu Li, Zhen Cao, Yuxing Peng, Lei Liu, Yonglong Wang, Shu Wang, Ji-Qiang Wang, Tianying Yan, Xue-Ping Gao, De- Ying Song and Pan-Wen .. Journal of Fluorine Chemistry , Nature Communications volume 7, Article number: () | Download Citation . (d) Data sets cover a range of detector types, including Area Welberry, T. Diffuse X-Ray Scattering and Models of Disorder OUP Oxford () . . Chinese Academy of Sciences, Shanghai , China. Ming Lei.

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Details of these FP measurements are presented as Supplemental Information. For all FP-binding assays, fluorescence intensity FI and FP were measured after 50 minutes of incubation at room temperature to ensure equilibrium measurements. The Base Case Gutterod E. Effects of the functionalization of the ordered mesoporous carbon support surface on iron catalysts for the Fischer—Tropsch 18082 of Lower Olefins Oschatz M.

Panel d also shows an orientation rotated by deg, revealing no significant CSPs on the opposite side of the molecule.

Xiao for dr discussions and comments on this manuscript. Structural basis for suppression of a host antiviral response by influenza A virus. Robotic cloning and protein production platform of the Northeast Structural Genomics Consortium. Investigating lej interstellar dust through the Fe K-edge Rogantini D. While dimerization mediated by the CTD of NS1B is not required for binding small RNA substrates, our observation that virus replication is attenuated fold by a dimer-disrupting RA mutation suggests that dimerization of full-length NS1B mediated by its CTD may none-the-less contribute to the efficiency of viral replication.

These biophysical studies demonstrate that the NS1B 1882 has a weak propensity to form a homodimeric structure with the same interface observed in the X-ray crystal structure. National Center for Biotechnology InformationU. SUMO fusion technology for enhanced protein production in prokaryotic and eukaryotic expression systems.

Unexpected RNA-binding site in the NS1B Protein from Influenza B Virus not present in NS1A

Sequence-specific resonance assignments and chemical shift perturbation studies were carried out using standard methods, outlined in Supplemental Information.

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We demonstrate that single-site alanine replacements of basic residues in this site lead to reduced RNA-binding activity, and that recombinant influenza B viruses expressing these mutant NS1B proteins are severely attenuated in replication. Structure determination and refinement At the home X-ray source wavelength 1.

Jahn-Teller distortion driven magnetic polarons in magnetite Huang H. Associated Data Supplementary Materials.

This is a classic example in which the three-dimensional protein structure provides evidence for an unexpected and important biological function, which was then validated first by biophysical studies with purified protein samples, followed by the generation of viruses bearing specific mutations.

Details of sample preparation for crystallization, nucleic acid binding, and NMR studies, including procedures for production of isotope-enriched samples, are presented as Supplemental Information.

The structural and biophysical results outlined above reveal a novel, unanticipated RNA binding function in the C-terminal domain of the NS1 protein of influenza B viruses. Nat Struct Mol Biol. Most importantly, this study reveals an unexpected RNA-binding function in the C-terminal domain of NS1B, a novel function that distinguishes influenza B viruses from influenza A viruses.

B01882DOI: Author information Copyright and License information Disclaimer. The NS1 proteins of influenza A and B strains bind some common host factors; e. The key basic residues responsible for RNA-binding activity are shown in green in Figs. The platinum rush Jong de K. Where indicated, d cell extracts were analyzed by immunoblots using antibodies against the viral M1 protein Southern Biotech and NS1B protein.

The monomeric form of the NS1B CTD is sufficient to bind RNA Dimeric interactions observed in crystal structures may or may not occur in solution, particularly under dilute protein conditions.

In addition, some residues shown in white in Figure 1b within the apparent binding site did not provide reliable CSP li, or are prolines which lack 15 N- 1 H resonances. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final citable form.

Unexpected RNA-binding site in the NS1B Protein from Influenza B Virus not present in NS1A

Lary of the University of Connecticut Analytical Ultracentrafugation Facility for providing analytical ultracentrifugation analysis, and Dr. Group publications Manufacture of highly loaded silica-supported cobalt Fischer — Tropsch catalysts from a metal organic framework Sun X.

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They form a largely basic patch on the surface of the protein structure, and are highly conserved across influenza B NS1B proteins Supplemental Figure S1b. The NS1 protein of influenza A virus NS1A protein has been se studied and shown to have multiple functions that counter host antiviral responses and regulate other cellular and viral functions Krug and Garcia-Sastre, The high-throughput protein sample production platform of the Northeast Structural Genomics Consortium.

Group publications – Inorganic Chemistry and Catalysis

However, using a structure-based sequence alignment, the corresponding residues in influenza A NS1A proteins are neither basic nor conserved cf.

In the crystal structure, residues R and R are involved in intermolecular salt bridges with residues N and E, respectively, at the ,ei interface Figure 3c. Critical questions in the field of influenza virus research involve elucidating the features of influenza A and leo B viruses that distinguish their infection mechanism s and virulence. Infection by each of these influenza B viruses caused activation of IRF3 at early times 2—4 hours postinfectiontriggered directly by the incoming virus Makela et al.

Author manuscript; available in PMC Sep 6. The molecular orientations in panels abcand d-left are the same. Less extensive chemical shift perturbations are also observed on this same face of the NS1 CTD molecule upon binding a single-strand nt RNA substrate data not shown. Rescue of influenza B virus from eight plasmids. Amino-acid residues in the basic surface and in an adjacent acid patch, identified in the X-ray crystal structure exhibit backbone 15 N- 1 H chemical shift perturbations upon binding of this mer dsRNA Figure 1ddemonstrating that the RNA-binding site in the NS1B CTD involves the conserved basic surface observed in the X-ray crystal structure Figure 1b.

An amino-terminal polypeptide fragment of the influenza virus NS1 protein possesses specific RNA-binding activity and largely helical backbone structure. Acknowledgments We thank Drs. Evaluating protein structures determined by structural genomics consortia. 204 interface of the effector domain of non-structural protein 1 from influenza A virus: