Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH

Aggregation of eye lens proteins leads to cataracts, a major cause of blindness. Here the authors use solid state NMR to probe the structure of γD-crystallin eye lens proteins aggregates, which are found to retain a native-like conformation.

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Autores principales:	Jennifer C. Boatz, Matthew J. Whitley, Mingyue Li, Angela M. Gronenborn, Patrick C. A. van der Wel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/194e190adbbb4cf7b1a9b3aaf854fa91
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spelling	oai:doaj.org-article:194e190adbbb4cf7b1a9b3aaf854fa912021-12-02T15:36:59ZCataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH10.1038/ncomms151372041-1723https://doaj.org/article/194e190adbbb4cf7b1a9b3aaf854fa912017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15137https://doaj.org/toc/2041-1723Aggregation of eye lens proteins leads to cataracts, a major cause of blindness. Here the authors use solid state NMR to probe the structure of γD-crystallin eye lens proteins aggregates, which are found to retain a native-like conformation.Jennifer C. BoatzMatthew J. WhitleyMingyue LiAngela M. GronenbornPatrick C. A. van der WelNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jennifer C. Boatz Matthew J. Whitley Mingyue Li Angela M. Gronenborn Patrick C. A. van der Wel Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH
description	Aggregation of eye lens proteins leads to cataracts, a major cause of blindness. Here the authors use solid state NMR to probe the structure of γD-crystallin eye lens proteins aggregates, which are found to retain a native-like conformation.
format	article
author	Jennifer C. Boatz Matthew J. Whitley Mingyue Li Angela M. Gronenborn Patrick C. A. van der Wel
author_facet	Jennifer C. Boatz Matthew J. Whitley Mingyue Li Angela M. Gronenborn Patrick C. A. van der Wel
author_sort	Jennifer C. Boatz
title	Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH
title_short	Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH
title_full	Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH
title_fullStr	Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH
title_full_unstemmed	Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH
title_sort	cataract-associated p23t γd-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological ph
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/194e190adbbb4cf7b1a9b3aaf854fa91
work_keys_str_mv	AT jennifercboatz cataractassociatedp23tgdcrystallinretainsanativelikefoldinamorphouslookingaggregatesformedatphysiologicalph AT matthewjwhitley cataractassociatedp23tgdcrystallinretainsanativelikefoldinamorphouslookingaggregatesformedatphysiologicalph AT mingyueli cataractassociatedp23tgdcrystallinretainsanativelikefoldinamorphouslookingaggregatesformedatphysiologicalph AT angelamgronenborn cataractassociatedp23tgdcrystallinretainsanativelikefoldinamorphouslookingaggregatesformedatphysiologicalph AT patrickcavanderwel cataractassociatedp23tgdcrystallinretainsanativelikefoldinamorphouslookingaggregatesformedatphysiologicalph
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Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH

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