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  1. B100 理学部/理学研究科
  2. B100a 雑誌掲載論文
  3. 学術雑誌

Structural basis for the regulation of nuclear import of Epstein-Barr virus nuclear antigen 1 (EBNA1) by phosphorylation of the nuclear localization signal

http://hdl.handle.net/2237/26586
http://hdl.handle.net/2237/26586
d02ffd9f-ba66-44b9-a6f8-22c1abf5d401
名前 / ファイル ライセンス アクション
Nakada2017BBRC_for_depository.pdf Nakada2017BBRC_for_depository.pdf ファイル公開:2018/02/26 (2.7 MB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2017-06-07
タイトル
タイトル Structural basis for the regulation of nuclear import of Epstein-Barr virus nuclear antigen 1 (EBNA1) by phosphorylation of the nuclear localization signal
言語 en
著者 Nakada, Ryohei

× Nakada, Ryohei

WEKO 72193

en Nakada, Ryohei

Search repository
Hirano, Hidemi

× Hirano, Hidemi

WEKO 72194

en Hirano, Hidemi

Search repository
Matsuura, Yoshiyuki

× Matsuura, Yoshiyuki

WEKO 72195

en Matsuura, Yoshiyuki

Search repository
アクセス権
アクセス権 open access
アクセス権URI http://purl.org/coar/access_right/c_abf2
権利
言語 en
権利情報 © 2017. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
抄録
内容記述 Epstein-Barr virus (EBV) nuclear antigen 1 (EBNA1) is expressed in every EBV-positive tumor and is essential for the maintenance, replication, and transcription of the EBV genome in the nucleus of host cells. EBNA1 is a serine phosphoprotein, and it has been shown that phosphorylation of S385 in the nuclear localization signal (NLS) of EBNA1 increases the binding affinity to the nuclear import adaptor importin-α1 as well as importin-α5, and stimulates nuclear import of EBNA1. To gain insights into how phosphorylation of the EBNA1 NLS regulates nuclear import, we have determined the crystal structures of two peptide complexes of importin-α1: one with S385-phosphorylated EBNA1 NLS peptide, determined at 2.0 Å resolution, and one with non-phosphorylated EBNA1 NLS peptide, determined at 2.2 Å resolution. The structures show that EBNA1 NLS binds to the major and minor NLS-binding sites of importin-α1, and indicate that the binding affinity of the EBNA1 NLS to the minor NLS-binding site could be enhanced by phosphorylation of S385 through electrostatic interaction between the phosphate group of phospho-S385 and K392 of importin-α1 (corresponding to R395 of importin-α5) on armadillo repeat 8.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 Elsevier
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
出版タイプ
出版タイプ AM
出版タイプResource http://purl.org/coar/version/c_ab4af688f83e57aa
DOI
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 https://doi.org/10.1016/j.bbrc.2017.01.063
ISSN
収録物識別子タイプ PISSN
収録物識別子 0006-291X
書誌情報 en : Biochemical and Biophysical Research Communications

巻 484, 号 1, p. 113-117, 発行日 2017-02-26
著者版フラグ
値 author
URI
識別子 https://doi.org/10.1016/j.bbrc.2017.01.063
識別子タイプ DOI
URI
識別子 http://hdl.handle.net/2237/26586
識別子タイプ HDL
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