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Crystal structure of importin‐α bound to the nuclear localization signal of Epstein‐Barr virus EBNA‐LP protein
Author(s) -
Nakada Ryohei,
Matsuura Yoshiyuki
Publication year - 2017
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3173
Subject(s) - nls , nuclear localization sequence , importin , arginine , nuclear transport , signal transducing adaptor protein , lysine , chemistry , biology , biophysics , microbiology and biotechnology , cell nucleus , biochemistry , amino acid , signal transduction , nucleus
Epstein‐Barr virus EBNA‐LP protein is a transcriptional coactivator of EBNA2. Efficient nuclear localization of EBNA‐LP is essential for cooperation with EBNA2. Here, we report the crystal structure of the nuclear import adaptor importin‐α1 bound to the nuclear localization signal (NLS) of EBNA‐LP that shows EBNA‐LP residues 44‐RRVRRR‐49 binding to the major NLS‐binding site at the P0‐P5 positions. In contrast to previously characterized classical NLSs that invariably have a basic residue [either lysine (in the vast majority of cases) or arginine] at the P2 position, the EBNA‐LP NLS is unique in that it has valine at the P2 position. The loss of the critical P2 lysine (or arginine) is compensated by arginine at the P0 position in the EBNA‐LP NLS.