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

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
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Acceso en línea:https://doaj.org/article/c01ab08a88114dd8bdfe140a87d7b465
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Sumario: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.

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