4.7 Article

NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH 6.5

Journal

JOURNAL OF MOLECULAR BIOLOGY
Volume 402, Issue 4, Pages 619-628

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2010.07.043

Keywords

severe acute respiratory syndrome; coronavirus; nsp7; NMR structure; conformational polymorphism

Funding

  1. National Institute of Allergy and Infectious Diseases/National Institutes of Health [HHSN266200400058C]
  2. Joint Center for Structural Genomics through National Institutes of Health/National institute of General Medical Sciences [U54-GM074898]
  3. Latvian Institute of Organic Synthesis

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The NMR structure of the severe acute respiratory syndrome coronavirus nonstructural protein (nsp) 7 in aqueous solution at pH 6.5 was determined and compared with the results of previous structure determinations of nsp7 in solution at pH 7.5 and in the crystals of a hexadecameric nsp7/nsp8 complex obtained from a solution at pH 7.5. All three structures contain four helices as the only regular secondary structures, but there are differences in the lengths and sequence locations of the four helices, as well as between the tertiary folds. The present study includes data on conformational equilibria and intramolecular rate processes in nsp7 in solution at pH 6.5, which provide further insights into the polymorphisms implicated by a comparison of the three presently available nsp7 structures. (C) 2010 Elsevier Ltd. All rights reserved.

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