Structural Fine-Tuning of MIT-Interacting Motif 2 (MIM2) and Allosteric Regulation of ESCRT-III by Vps4 in Yeast
详细信息 查看全文
- 作者：Rieko Kojima1 ; Takayuki Obita ; obita@pha.u-toyama.ac.jp" class="auth_mail" title="E-mail the corresponding author ; Kousuke Onoue ; Mineyuki Mizuguchi
- 关键词：ESCRT ; endosomal sorting complexes required for transport ; Vps ; vacuolar protein sorting ; Vfa ; Vps four-associated
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：5 June 2016
- 年：2016
- 卷：428
- 期：11
- 页码：2392-2404
- 全文大小：1525 K
文摘
- class="listitem" id="list_l0005">
- class="label">•
The crystal structure of Vps4 in complex with Vps20 from Saccharomyces cerevisiae was determined.
- class="label">•
Vps4 recognizes ESCRT-III in an allosteric manner.
- class="label">•
The MIM2 consensus sequence was refined.
- class="label">•
Vps20 adopts a short-helix and non-canonical MIM2 with a bulge upon binding to Vps4.