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Author Notes:

YM, miao@ku.edu

BL, bo.liang@emory.edu

Y.G., D.C., Y.M., and B.L. designed and executed the experiments. Y.G. purified M2-1 proteins, assembled and crystallized the M2-1:SH7 complex, and collected and processed the data. H.M.A., A.Swain, A.Y., and A.Salazar purified WT and mutant proteins and set up crystallization trails. S.H. and C.O. examined crystals and optimized crystals. P.P. and A.B. made mutant clones. J.M.H. prepared crystallization solutions. B.L. built and refined the model. S.P. and K.P.J. performed and analyzed simulations. B.L. supervised and coordinated the project. B.L., Y.M., and Y.G. wrote the manuscript. B.L. and Y.M. revised the manuscript.

The crystallographic data were collected at the Southeast Regional Collaborative Access Team (SER-CAT) 22-ID beamline at the Advanced Photon Source, Argonne National Laboratory, which was supported by the United States Department of Energy, Office of Science, Office of Basic Energy Sciences, under contract W-31-109-Eng-38. B.L. was supported by NIGMS R01GM130950 and the Start-Up Fund from Emory University School of Medicine. Y.M. was supported by the startup funding in the College of Liberal Arts and Sciences at the University of Kansas. We want to thank Dr. Karen Kirby for the MST training and Dr. Stefan Sarafianos to allow us to use the MST instrument. We want to thank the members of the Liang group at Emory University School of Medicine for performing the experimental studies, including the crystallographic, mutagenesis, and MST assays, and the members of the Miao group at the University of Kansas for computational simulations.

The authors declare no competing interests.

Subject:

Keywords:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Biochemistry & Molecular Biology
  • Biophysics
  • Cell Biology
  • ACCELERATED MOLECULAR-DYNAMICS
  • TRANSCRIPTION TERMINATION
  • ACTIVATION
  • CHARMM
  • PHOSPHORYLATION
  • REPLICATION
  • SIMULATIONS
  • MUTATIONS
  • STABILITY
  • JUNCTIONS

Structure of the Human Respiratory Syncytial Virus M2-1 Protein in Complex with a Short Positive-Sense Gene-End RNA

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Tools:

Journal Title:

STRUCTURE

Volume:

Volume 28, Number 9

Publisher:

, Pages 979-+

Type of Work:

Article | Post-print: After Peer Review

Abstract:

Gao et al. determined a 2.7-Å resolution crystal structure of human respiratory syncytial virus (HRSV) M2-1 protein in complex with a short positive-sense gene-end RNA. Gaussian accelerated molecular dynamics (GaMD) simulations captured spontaneous binding of RNA to M2-1. The results provided a structural basis for RNA recognition by M2-1.

Copyright information:

This is an Open Access work distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License (https://creativecommons.org/licenses/by-nc-nd/4.0/rdf).
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