NDLI: Rapid amyloid fiber formation from the fast-folding WW domain FBP28

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Rapid amyloid fiber formation from the fast-folding WW domain FBP28

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Petrovich, Miriana Sharpe, Timothy D. Finch, John T. Berriman, John Fersht, Alan R. Ferguson, Neil
Description	Author Affiliation: Ferguson N ( Medical Research Council Centre for Protein Engineering, Medical Research Council Centre, Hills Road, Cambridge CB2 2QH, UK.);
Abstract	The WW domains are small proteins that contain a three-stranded, antiparallel beta-sheet. The 40-residue murine FBP28 WW domain rapidly formed twirling ribbon-like fibrils at physiological temperature and pH, with morphology typical of amyloid fibrils. These ribbons were unusually wide and well ordered, making them highly suitable for structural studies. Their x-ray and electron-diffraction patterns displayed the characteristic amyloid fiber 0.47-nm reflection of the cross-beta diffraction signature. Both conventional and electron cryomicroscopy showed clearly that the ribbons were composed of many 2.5-nm-wide subfilaments that ran parallel to the long axis of the fiber. There was a region of lower density along the center of each filament. Lateral association of these filaments generated twisted, often interlinked, sheets up to 40 nm wide and many microns in length. The pitch of the helix varied from 60 to 320 nm, depending on the width of the ribbon. The wild-type FBP28 fibers were formed under conditions in which multiexponential folding kinetics is observed in other studies and which was attributed to a change in the mechanism of folding. It is more likely that those phases result from initial events in the off-pathway aggregation observed here.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Amyloid Chemistry Metabolism Carrier Proteins Ultrastructure Animals In Vitro Techniques Kinetics Macromolecular Substances Mice Microscopy, Electron Models, Molecular Protein Folding Protein Structure, Secondary Protein Structure, Tertiary Scattering, Radiation Transcriptional Elongation Factors X-Ray Diffraction Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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