Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ

The proteasome activator PA28αβ affects MHC class I antigen presentation by associating with immunoproteasome core particles (iCPs). Cryo-EM structures of the mammalian PA28αβ -iCP immunoproteasome and free iCP, combined with cross-linking data, reveal the complex architecture and suggest a distinct...

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Autores principales: Jinhuan Chen, Yifan Wang, Cong Xu, Kaijian Chen, Qiaoyu Zhao, Shutian Wang, Yue Yin, Chao Peng, Zhanyu Ding, Yao Cong
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Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/aa03cc969f924ebc806c416e0c938a9d
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spelling oai:doaj.org-article:aa03cc969f924ebc806c416e0c938a9d2021-12-02T14:06:10ZCryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ10.1038/s41467-021-21028-32041-1723https://doaj.org/article/aa03cc969f924ebc806c416e0c938a9d2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21028-3https://doaj.org/toc/2041-1723The proteasome activator PA28αβ affects MHC class I antigen presentation by associating with immunoproteasome core particles (iCPs). Cryo-EM structures of the mammalian PA28αβ -iCP immunoproteasome and free iCP, combined with cross-linking data, reveal the complex architecture and suggest a distinct immunoproteasome activation mechanism.Jinhuan ChenYifan WangCong XuKaijian ChenQiaoyu ZhaoShutian WangYue YinChao PengZhanyu DingYao CongNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Jinhuan Chen
Yifan Wang
Cong Xu
Kaijian Chen
Qiaoyu Zhao
Shutian Wang
Yue Yin
Chao Peng
Zhanyu Ding
Yao Cong
Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ
description The proteasome activator PA28αβ affects MHC class I antigen presentation by associating with immunoproteasome core particles (iCPs). Cryo-EM structures of the mammalian PA28αβ -iCP immunoproteasome and free iCP, combined with cross-linking data, reveal the complex architecture and suggest a distinct immunoproteasome activation mechanism.
format article
author Jinhuan Chen
Yifan Wang
Cong Xu
Kaijian Chen
Qiaoyu Zhao
Shutian Wang
Yue Yin
Chao Peng
Zhanyu Ding
Yao Cong
author_facet Jinhuan Chen
Yifan Wang
Cong Xu
Kaijian Chen
Qiaoyu Zhao
Shutian Wang
Yue Yin
Chao Peng
Zhanyu Ding
Yao Cong
author_sort Jinhuan Chen
title Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ
title_short Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ
title_full Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ
title_fullStr Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ
title_full_unstemmed Cryo-EM of mammalian PA28αβ-iCP immunoproteasome reveals a distinct mechanism of proteasome activation by PA28αβ
title_sort cryo-em of mammalian pa28αβ-icp immunoproteasome reveals a distinct mechanism of proteasome activation by pa28αβ
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/aa03cc969f924ebc806c416e0c938a9d
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