Open AccessCrystallization and preliminary X‐ray analysis of Ebola VP35 interferon inhibitory domain mutant proteins
Author(s) -
Leung Daisy W.,
Borek Dominika,
Farahbakhsh Mina,
Ramanan Parameshwaran,
Nix Jay C.,
Wang Tianjiao,
Prins Kathleen C.,
Otwinowski Zbyszek,
Honzatko Richard B.,
Helgeson Luke A.,
Basler Christopher F.,
Amarasinghe Gaya K.
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110013266
Subject(s) - mutant , virology , interferon , crystallization , inhibitory postsynaptic potential , computational biology , chemistry , biology , biochemistry , gene , organic chemistry , neuroscience
VP35 is one of seven structural proteins encoded by the Ebola viral genome and mediates viral replication, nucleocapsid formation and host immune suppression. The C‐terminal interferon inhibitory domain (IID) of VP35 is critical for dsRNA binding and interferon inhibition. The wild‐type VP35 IID structure revealed several conserved residues that are important for dsRNA binding and interferon antagonism. Here, the expression, purification and crystallization of recombinant Zaire Ebola VP35 IID mutants R312A, K319A/R322A and K339A in space groups P 6 1 22, P 2 1 2 1 2 1 and P 2 1 , respectively, are described. Diffraction data were collected using synchrotron sources at the Advanced Light Source and the Advanced Photon Source.