Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome
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- 作者：Xiang Chen1 ; 4 ; Leah Randles1 ; 4 ; Ke Shi2 ; Sergey G. Tarasov3 ; Hideki Aihara2 ; Kylie J. Walters1 ; kylie.walters@nih.gov" class="auth_mail" title="E-mail the corresponding author
- 关键词：proteasome ; ubiquitin ; Rpn1 ; Rpn13 ; Dsk2 ; Rad23
- 刊名：Structure
- 出版年：2016
- 出版时间：2 August 2016
- 年：2016
- 卷：24
- 期：8
- 页码：1257-1270
- 全文大小：5278 K
文摘
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UBL shuttle factors bind to ubiquitin-interacting residues of proteasome receptors
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hRpn13:hPLIC2 structure reveals an optimized UBL for hRpn13 binding
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hPLIC2 sterically blocks Rpn13 binding to K48 diubiquitin, its preferred chain type
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Rpn1 T1:Rad23UBL structure reveals Rad23 binding to Helix28/Helix30 of Rpn1 T1