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Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2

Since its discovery, several ligands of the ZZ domain have been identified; however, molecular and structural information underlying binding of these ligands remains limited. Here, we describe a protocol for biochemical and structural analysis of the ZZ domain of human E3 ubiquitin ligase HERC2 (HER...

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Autores principales: Liu, Jiuyang, Xue, Zhaoyu, Vann, Kendra R., Shi, Xiaobing, Kutateladze, Tatiana G.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7757301/
https://www.ncbi.nlm.nih.gov/pubmed/33377049
http://dx.doi.org/10.1016/j.xpro.2020.100155
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author Liu, Jiuyang
Xue, Zhaoyu
Vann, Kendra R.
Shi, Xiaobing
Kutateladze, Tatiana G.
author_facet Liu, Jiuyang
Xue, Zhaoyu
Vann, Kendra R.
Shi, Xiaobing
Kutateladze, Tatiana G.
author_sort Liu, Jiuyang
collection PubMed
description Since its discovery, several ligands of the ZZ domain have been identified; however, molecular and structural information underlying binding of these ligands remains limited. Here, we describe a protocol for biochemical and structural analysis of the ZZ domain of human E3 ubiquitin ligase HERC2 (HERC2(ZZ)) and its interaction with its ligands: the N-terminal tails of histone H3 and SUMO1. This methodology could be applied for characterization of binding activities of other histone readers. For complete details on the use and execution of this protocol, please refer to Liu et al. (2020).
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spelling pubmed-77573012020-12-28 Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2 Liu, Jiuyang Xue, Zhaoyu Vann, Kendra R. Shi, Xiaobing Kutateladze, Tatiana G. STAR Protoc Protocol Since its discovery, several ligands of the ZZ domain have been identified; however, molecular and structural information underlying binding of these ligands remains limited. Here, we describe a protocol for biochemical and structural analysis of the ZZ domain of human E3 ubiquitin ligase HERC2 (HERC2(ZZ)) and its interaction with its ligands: the N-terminal tails of histone H3 and SUMO1. This methodology could be applied for characterization of binding activities of other histone readers. For complete details on the use and execution of this protocol, please refer to Liu et al. (2020). Elsevier 2020-10-28 /pmc/articles/PMC7757301/ /pubmed/33377049 http://dx.doi.org/10.1016/j.xpro.2020.100155 Text en © 2020 The Author(s) http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Protocol
Liu, Jiuyang
Xue, Zhaoyu
Vann, Kendra R.
Shi, Xiaobing
Kutateladze, Tatiana G.
Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2
title Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2
title_full Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2
title_fullStr Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2
title_full_unstemmed Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2
title_short Protocol for Biochemical Analysis and Structure Determination of the ZZ Domain of the E3 Ubiquitin Ligase HERC2
title_sort protocol for biochemical analysis and structure determination of the zz domain of the e3 ubiquitin ligase herc2
topic Protocol
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7757301/
https://www.ncbi.nlm.nih.gov/pubmed/33377049
http://dx.doi.org/10.1016/j.xpro.2020.100155
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