Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein.

Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein. Research Abstract Details 

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Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein. Abstract Text:

Gareth J Morgan,Silva Giannini,Andrea M Hounslow,C Jeremy Craven,Eva Zerovnik,Vito Turk,Jonathan P Waltho,Rosemary A Staniforth,Gareth J Morgan,Silva Giannini,Andrea M Hounslow,C Jeremy Craven,Eva Zerovnik,Vito Turk,Jonathan P Waltho,Rosemary A Staniforth,

Members of the cystatin superfamily are involved in an inherited form of cerebral amyloid angiopathy and readily form amyloid fibrils in vitro. We have determined the structured core of human stefin B (cystatin B) amyloid fibrils using quenched hydrogen exchange and NMR. The core contains residues from four of the five strands of the native beta-sheet, delimited by unprotected loop regions analogous to those of the native monomeric structure. However, non-native features are also apparent, the most striking of which is the exclusion of the native alpha-helix. Before forming amyloid in vitro, cystatins dimerise via 3D domain swapping, and assemble into tetramers with trans to cis isomerism of a conserved proline. In the fibril, the hinge loop that forms an extended beta-structure in the dimer remains protected, consistent with the domain-swapping interface being maintained. However, the fibril data are not compatible with a simple 3D domain-swapping model for amyloid formation, and the displacement of the helix points to alternative packing arrangements of native-like beta-structure, in which proline isomerism is important in preventing steric clashing.

Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein. Publishing Authors By Initials

GJ Morgan,S Giannini,AM Hounslow,CJ Craven,E Zerovnik,V Turk,JP Waltho,RA Staniforth,GJ Morgan,S Giannini,AM Hounslow,CJ Craven,E Zerovnik,V Turk,JP Waltho,RA Staniforth,

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Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of molecular biology

VOLUME: 375

Page Numbers: 487-98

Journal Abbreviation: J. Mol. Biol.

ISSN: 1089-8638

DAY: 22

MONTH: 10

YEAR: 2007

Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein. Information

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LANGUAGE: eng

NlmUniqueID: 2985088

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Grant and Affiliation Information for Exclusion of the native alpha-helix from the amyloid fibrils of a mixed alpha/beta protein.

AFFILIATION: Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, S10 2TN, UK.

Country: England

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MEDLINETA: J Mol Biol

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