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Crystal structure of the Nipah virus phosphoprotein tetramerization domain

Academic Article
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Overview

related to degree

  • Bruhn, Jessica, Ph.D. in Biophysics, Scripps Research 2011 - 2016

authors

  • Bruhn, Jessica
  • Barnett, K. C.
  • Bibby, J.
  • Thomas, J. M. H.
  • Keegan, R. M.
  • Rigden, D. J.
  • Bornholdt, Zachary
  • Saphire, Erica Ollmann

publication date

  • January 2014

journal

  • Journal of Virology  Journal

abstract

  • The Nipah virus phosphoprotein (P) is multimeric and tethers the viral polymerase to the nucleocapsid. We present the crystal structure of the multimerization domain of Nipah virus P: a long, parallel, tetrameric, coiled coil with a small, α-helical cap structure. Across the paramyxoviruses, these domains share little sequence identity yet are similar in length and structural organization, suggesting a common requirement for scaffolding or spatial organization of the functions of P in the virus life cycle.

subject areas

  • Biopolymers
  • Crystallography, X-Ray
  • Nipah Virus
  • Phosphoproteins
  • Protein Conformation
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Identity

PubMed Central ID

  • PMC3911761

International Standard Serial Number (ISSN)

  • 0022-538X

Digital Object Identifier (DOI)

  • 10.1128/jvi.02294-13

PubMed ID

  • 24155387
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Additional Document Info

start page

  • 758

end page

  • 762

volume

  • 88

issue

  • 1

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