Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection

Major Histocompatibility Complex (MHC) class I molecules present tightly binding peptides on the cell surface for recognition by cytotoxic T cells. Here, the authors present the crystal structures of a disulfide-stabilized human MHC class I molecule in the peptide-free state and bound with dipeptide...

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Autores principales:	Raghavendra Anjanappa, Maria Garcia-Alai, Janine-Denise Kopicki, Julia Lockhauserbäumer, Mohamed Aboelmagd, Janina Hinrichs, Ioana Maria Nemtanu, Charlotte Uetrecht, Martin Zacharias, Sebastian Springer, Rob Meijers
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/0a9d6a6f48e3448e84d9257ff4977dbc
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spelling	oai:doaj.org-article:0a9d6a6f48e3448e84d9257ff4977dbc2021-12-02T14:41:22ZStructures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection10.1038/s41467-020-14862-42041-1723https://doaj.org/article/0a9d6a6f48e3448e84d9257ff4977dbc2020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14862-4https://doaj.org/toc/2041-1723Major Histocompatibility Complex (MHC) class I molecules present tightly binding peptides on the cell surface for recognition by cytotoxic T cells. Here, the authors present the crystal structures of a disulfide-stabilized human MHC class I molecule in the peptide-free state and bound with dipeptides, and find that peptide binding is accompanied by concerted conformational switches of the amino acid side chains in the binding pockets.Raghavendra AnjanappaMaria Garcia-AlaiJanine-Denise KopickiJulia LockhauserbäumerMohamed AboelmagdJanina HinrichsIoana Maria NemtanuCharlotte UetrechtMartin ZachariasSebastian SpringerRob MeijersNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-11 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Raghavendra Anjanappa Maria Garcia-Alai Janine-Denise Kopicki Julia Lockhauserbäumer Mohamed Aboelmagd Janina Hinrichs Ioana Maria Nemtanu Charlotte Uetrecht Martin Zacharias Sebastian Springer Rob Meijers Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection
description	Major Histocompatibility Complex (MHC) class I molecules present tightly binding peptides on the cell surface for recognition by cytotoxic T cells. Here, the authors present the crystal structures of a disulfide-stabilized human MHC class I molecule in the peptide-free state and bound with dipeptides, and find that peptide binding is accompanied by concerted conformational switches of the amino acid side chains in the binding pockets.
format	article
author	Raghavendra Anjanappa Maria Garcia-Alai Janine-Denise Kopicki Julia Lockhauserbäumer Mohamed Aboelmagd Janina Hinrichs Ioana Maria Nemtanu Charlotte Uetrecht Martin Zacharias Sebastian Springer Rob Meijers
author_facet	Raghavendra Anjanappa Maria Garcia-Alai Janine-Denise Kopicki Julia Lockhauserbäumer Mohamed Aboelmagd Janina Hinrichs Ioana Maria Nemtanu Charlotte Uetrecht Martin Zacharias Sebastian Springer Rob Meijers
author_sort	Raghavendra Anjanappa
title	Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection
title_short	Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection
title_full	Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection
title_fullStr	Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection
title_full_unstemmed	Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection
title_sort	structures of peptide-free and partially loaded mhc class i molecules reveal mechanisms of peptide selection
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/0a9d6a6f48e3448e84d9257ff4977dbc
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Structures of peptide-free and partially loaded MHC class I molecules reveal mechanisms of peptide selection

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