Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity

The aggregation prone D76N beta-2 microglobulin mutant causes systemic amyloidosis. Here the authors combine crystallography, solid-state NMR, and computational studies and show that the D76N mutation increases protein dynamics and destabilizes the outer strands, which leads to an exposure of amyloi...

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Autores principales:	Tanguy Le Marchand, Matteo de Rosa, Nicola Salvi, Benedetta Maria Sala, Loren B. Andreas, Emeline Barbet-Massin, Pietro Sormanni, Alberto Barbiroli, Riccardo Porcari, Cristiano Sousa Mota, Daniele de Sanctis, Martino Bolognesi, Lyndon Emsley, Vittorio Bellotti, Martin Blackledge, Carlo Camilloni, Guido Pintacuda, Stefano Ricagno
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c01ab08a88114dd8bdfe140a87d7b465
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spelling	oai:doaj.org-article:c01ab08a88114dd8bdfe140a87d7b4652021-12-02T15:34:03ZConformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity10.1038/s41467-018-04078-y2041-1723https://doaj.org/article/c01ab08a88114dd8bdfe140a87d7b4652018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04078-yhttps://doaj.org/toc/2041-1723The aggregation prone D76N beta-2 microglobulin mutant causes systemic amyloidosis. Here the authors combine crystallography, solid-state NMR, and computational studies and show that the D76N mutation increases protein dynamics and destabilizes the outer strands, which leads to an exposure of amyloidogenic parts explaining its aggregation propensity.Tanguy Le MarchandMatteo de RosaNicola SalviBenedetta Maria SalaLoren B. AndreasEmeline Barbet-MassinPietro SormanniAlberto BarbiroliRiccardo PorcariCristiano Sousa MotaDaniele de SanctisMartino BolognesiLyndon EmsleyVittorio BellottiMartin BlackledgeCarlo CamilloniGuido PintacudaStefano RicagnoNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tanguy Le Marchand Matteo de Rosa Nicola Salvi Benedetta Maria Sala Loren B. Andreas Emeline Barbet-Massin Pietro Sormanni Alberto Barbiroli Riccardo Porcari Cristiano Sousa Mota Daniele de Sanctis Martino Bolognesi Lyndon Emsley Vittorio Bellotti Martin Blackledge Carlo Camilloni Guido Pintacuda Stefano Ricagno Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity
description	The aggregation prone D76N beta-2 microglobulin mutant causes systemic amyloidosis. Here the authors combine crystallography, solid-state NMR, and computational studies and show that the D76N mutation increases protein dynamics and destabilizes the outer strands, which leads to an exposure of amyloidogenic parts explaining its aggregation propensity.
format	article
author	Tanguy Le Marchand Matteo de Rosa Nicola Salvi Benedetta Maria Sala Loren B. Andreas Emeline Barbet-Massin Pietro Sormanni Alberto Barbiroli Riccardo Porcari Cristiano Sousa Mota Daniele de Sanctis Martino Bolognesi Lyndon Emsley Vittorio Bellotti Martin Blackledge Carlo Camilloni Guido Pintacuda Stefano Ricagno
author_facet	Tanguy Le Marchand Matteo de Rosa Nicola Salvi Benedetta Maria Sala Loren B. Andreas Emeline Barbet-Massin Pietro Sormanni Alberto Barbiroli Riccardo Porcari Cristiano Sousa Mota Daniele de Sanctis Martino Bolognesi Lyndon Emsley Vittorio Bellotti Martin Blackledge Carlo Camilloni Guido Pintacuda Stefano Ricagno
author_sort	Tanguy Le Marchand
title	Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity
title_short	Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity
title_full	Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity
title_fullStr	Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity
title_full_unstemmed	Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity
title_sort	conformational dynamics in crystals reveal the molecular bases for d76n beta-2 microglobulin aggregation propensity
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/c01ab08a88114dd8bdfe140a87d7b465
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Conformational dynamics in crystals reveal the molecular bases for D76N beta-2 microglobulin aggregation propensity

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