Molecular Mechanism of HIV-1 Vpr for Binding to Importin-α
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- 作者：Hideyuki Miyatake1 ; miyatake@riken.jp" class="auth_mail" title="E-mail the corresponding author ; Akira Sanjoh2 ; Tomoyuki Murakami3 ; Hironobu Murakami3 ; Go Matsuda3 ; Kyoji Hagiwara3 ; Masaru Yokoyama4 ; Hironori Sato4 ; Yoichi Miyamoto5 ; Naoshi Dohmae6 ; Yoko Aida3 ; aida@riken.jp" class="auth_mail" title="E-mail the corresponding author
- 关键词：Vpr ; viral protein R ; HIV-1 ; human immunodeficiency virus type 1 ; NLS ; nuclear localization signal ; h-importin-α1 ; human importin-α1 ; IBB ; importin-β-binding ; ARM ; armadillo ; GST ; glutathione S-transferase ; ITC ; isothermal titration calorimetry ; DLS ; dynamic light scattering ; PBS ; phosphate-buffered saline
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：3 July 2016
- 年：2016
- 卷：428
- 期：13
- 页码：2744-2757
- 全文大小：1821 K
文摘
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Crystal complex structure of HIV-1 Vpr C-terminal and importin-α
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Vpr C-terminal loop makes a twisted β-turn upon binding to importin-α, inducing homodimerization of importin-α.
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The twisted β-turn mimics a canonical NLS-binding motif for the minor NLS-binding site of importin-α.
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The major NLS-binding site free from the Vpr binding passively serves as the canonical NLS-binding site during pre-integration complex nuclear import.