Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease

ABCA4 is an ATP-binding cassette (ABC) transporter that flips N-retinylidenephosphatidylethanolamine (N-Ret-PE) to the cytoplasmic leaflet of photoreceptor membranes. ABCA4 mutations are associated with loss of vision. Here, structures of ABCA4 with and without substrate bound provide insight into N...

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Autores principales:	Jessica Fernandes Scortecci, Laurie L. Molday, Susan B. Curtis, Fabian A. Garces, Pankaj Panwar, Filip Van Petegem, Robert S. Molday
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c7f6dce4615b4c3fa5bb094bc2251eac
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spelling	oai:doaj.org-article:c7f6dce4615b4c3fa5bb094bc2251eac2021-12-02T18:37:16ZCryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease10.1038/s41467-021-26161-72041-1723https://doaj.org/article/c7f6dce4615b4c3fa5bb094bc2251eac2021-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26161-7https://doaj.org/toc/2041-1723ABCA4 is an ATP-binding cassette (ABC) transporter that flips N-retinylidenephosphatidylethanolamine (N-Ret-PE) to the cytoplasmic leaflet of photoreceptor membranes. ABCA4 mutations are associated with loss of vision. Here, structures of ABCA4 with and without substrate bound provide insight into N-Ret-PE binding and suggest a lateral access mechanism.Jessica Fernandes ScortecciLaurie L. MoldaySusan B. CurtisFabian A. GarcesPankaj PanwarFilip Van PetegemRobert S. MoldayNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Jessica Fernandes Scortecci Laurie L. Molday Susan B. Curtis Fabian A. Garces Pankaj Panwar Filip Van Petegem Robert S. Molday Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease
description	ABCA4 is an ATP-binding cassette (ABC) transporter that flips N-retinylidenephosphatidylethanolamine (N-Ret-PE) to the cytoplasmic leaflet of photoreceptor membranes. ABCA4 mutations are associated with loss of vision. Here, structures of ABCA4 with and without substrate bound provide insight into N-Ret-PE binding and suggest a lateral access mechanism.
format	article
author	Jessica Fernandes Scortecci Laurie L. Molday Susan B. Curtis Fabian A. Garces Pankaj Panwar Filip Van Petegem Robert S. Molday
author_facet	Jessica Fernandes Scortecci Laurie L. Molday Susan B. Curtis Fabian A. Garces Pankaj Panwar Filip Van Petegem Robert S. Molday
author_sort	Jessica Fernandes Scortecci
title	Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease
title_short	Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease
title_full	Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease
title_fullStr	Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease
title_full_unstemmed	Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease
title_sort	cryo-em structures of the abca4 importer reveal mechanisms underlying substrate binding and stargardt disease
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/c7f6dce4615b4c3fa5bb094bc2251eac
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Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease

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