Structural transitions in Orb2 prion-like domain relevant for functional aggregation in memory consolidation

The recent structural elucidation of ex vivo Drosophila Orb2 fibrils revealed a novel amyloid formed by interdigitated Gln and His residue side chains belonging to the prion-like domain. However, atomic-level details on the conformational transitions associated with memory consolidation remain unkno...

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Veröffentlicht in:	The Journal of biological chemistry 2020-12, Vol.295 (52), p.18122-18133
Hauptverfasser:	Oroz, Javier, Félix, Sara S., Cabrita, Eurico J., Laurents, Douglas V.
Format:	Artikel
Sprache:	eng
Schlagworte:	amyloid amyloidogenic proteins Animals Drosophila Drosophila - physiology Drosophila Proteins - chemistry Drosophila Proteins - metabolism functional amyloid intrinsically disordered protein Magnetic Resonance Spectroscopy Memory Consolidation metal ion-protein interaction mRNA Cleavage and Polyadenylation Factors - chemistry mRNA Cleavage and Polyadenylation Factors - metabolism NMR nuclear magnetic resonance pH regulation polyglutamine prion-like domain Prions - chemistry Protein Multimerization Protein Structure and Folding Transcription Factors - chemistry Transcription Factors - metabolism zinc
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