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Dynamics of the Intrinsically Disordered C‐Terminal Domain of the Nipah Virus Nucleoprotein and Interaction with the X Domain of the Phosphoprotein as Unveiled by NMR Spectroscopy
Author(s) -
Baronti Lorenzo,
Erales Jenny,
Habchi Johnny,
Felli Isabella C.,
Pierattelli Roberta,
Longhi Sonia
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402534
Subject(s) - phosphoprotein , nucleoprotein , hendra virus , nuclear magnetic resonance spectroscopy , crystallography , intrinsically disordered proteins , biophysics , chemistry , chemical shift , biology , stereochemistry , virus , biochemistry , phosphorylation , virology , dna , ebola virus
We provide an atomic‐resolution description based on NMR spectroscopy, of the intrinsically disordered C‐terminal domain of the Nipah virus nucleoprotein (N TAIL ), both in its isolated state and within the nucleocapsid (NC). Within the NC the second half of N TAIL retains conformational behavior similar to that of isolated N TAIL , whereas the first half of N TAIL becomes much more rigid. In spite of the mostly disordered nature of N TAIL , chemical shifts and relaxation measurements show a significant degree of α‐helical sampling in the molecular recognition element (MoRE) involved in binding to the X domain (XD) of the phosphoprotein, with this preconfiguration being more pronounced than in the N TAIL domain from the cognate Hendra virus. Outside the MoRE, an additional region exhibiting reduced flexibility was identified within N TAIL and found to be involved in binding to the XD. 1 H‐ and 13 C‐detected titration NMR experiments support a highly dynamic binding of N TAIL at the surface of the XD.