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Structural disorder within paramyxoviral nucleoproteins
Author(s) -
Longhi Sonia
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.05.055
Subject(s) - nucleoprotein , measles virus , biology , intrinsically disordered proteins , computational biology , virology , chemistry , genetics , biophysics , virus , measles , vaccination
In this review I summarize available data pointing to the abundance of structural disorder within the nucleoprotein (N) from three paramyxoviruses, namely the measles (MeV), Nipah (NiV) and Hendra (HeV) viruses. I provide a detailed description of the molecular mechanisms that govern the disorder‐to‐order transition that the intrinsically disordered C‐terminal domain (N TAIL ) of their N proteins undergoes upon binding to the C‐terminal X domain (XD) of the homologous phosphoproteins. I also show that a significant flexibility persists within N TAIL –XD complexes, which makes them illustrative examples of “fuzziness”. Finally, I discuss the functional implications of structural disorder for viral transcription and replication in light of the promiscuity of disordered regions and of the considerable reach they confer to the components of the replicative machinery.