Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism

The endoplasmic-reticulum aminopeptidase ERAP1 processes peptides for antigen presentation. Here, the authors assess ERAP1 conformational states in solution, providing insight into the molecular mechanisms of ERAP1 substrate-length dependent catalytic activity and regulation, including the effects o...

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Autores principales:	Zachary Maben, Richa Arya, Dimitris Georgiadis, Efstratios Stratikos, Lawrence J. Stern
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/746dd492c81545edb8b75082e4fb3cbb
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spelling	oai:doaj.org-article:746dd492c81545edb8b75082e4fb3cbb2021-12-02T17:19:39ZConformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism10.1038/s41467-021-25564-w2041-1723https://doaj.org/article/746dd492c81545edb8b75082e4fb3cbb2021-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25564-whttps://doaj.org/toc/2041-1723The endoplasmic-reticulum aminopeptidase ERAP1 processes peptides for antigen presentation. Here, the authors assess ERAP1 conformational states in solution, providing insight into the molecular mechanisms of ERAP1 substrate-length dependent catalytic activity and regulation, including the effects of autoimmune disease-associated polymorphism.Zachary MabenRicha AryaDimitris GeorgiadisEfstratios StratikosLawrence J. SternNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Zachary Maben Richa Arya Dimitris Georgiadis Efstratios Stratikos Lawrence J. Stern Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism
description	The endoplasmic-reticulum aminopeptidase ERAP1 processes peptides for antigen presentation. Here, the authors assess ERAP1 conformational states in solution, providing insight into the molecular mechanisms of ERAP1 substrate-length dependent catalytic activity and regulation, including the effects of autoimmune disease-associated polymorphism.
format	article
author	Zachary Maben Richa Arya Dimitris Georgiadis Efstratios Stratikos Lawrence J. Stern
author_facet	Zachary Maben Richa Arya Dimitris Georgiadis Efstratios Stratikos Lawrence J. Stern
author_sort	Zachary Maben
title	Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism
title_short	Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism
title_full	Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism
title_fullStr	Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism
title_full_unstemmed	Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism
title_sort	conformational dynamics linked to domain closure and substrate binding explain the erap1 allosteric regulation mechanism
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/746dd492c81545edb8b75082e4fb3cbb
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Conformational dynamics linked to domain closure and substrate binding explain the ERAP1 allosteric regulation mechanism

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