Common core structure of amyloid fibrils by synchrotron X-ray diffraction

被引：1440

作者：

Sunde, M ^{[1
]}

Serpell, LC ^{[1
]}

Bartlam, M ^{[1
]}

Fraser, PE ^{[1
]}

Pepys, MB ^{[1
]}

Blake, CCF ^{[1
]}

机构：

[1] UNIV OXFORD,MOL BIOPHYS LAB,OXFORD OX1 3QU,ENGLAND

来源：

JOURNAL OF MOLECULAR BIOLOGY | 1997年 / 273卷 / 03期

基金：

英国医学研究理事会;

关键词：

amyloid; fibre; X-ray diffraction; protofilament; structure;

D O I：

10.1006/jmbi.1997.1348

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Tissue deposition of normally soluble proteins as insoluble amyloid fibrils is associated with serious diseases including the systemic amyloidoses, maturity onset diabetes, Alzheimer's disease and transmissible spongiform encephalopathy. Although the precursor proteins in different diseases do not share sequence homology or related native structure, the morphology and properties of all amyloid fibrils are remarkably similar. Using intense synchrotron sources we observed that six different ex vivo amyloid fibrils and two synthetic fibril preparations all gave similar high-resolution X-ray fibre diffraction patterns, consistent with a helical array of beta-sheets parallel to the fibre long axis, with the strands perpen dicular to this axis. This confirms that amyloid fibrils comprise a structural superfamily and share a common protofilament substructure, irrespective of the nature of their precursor proteins. (C) 1997 Academic Press Limited.

引用

页码：729 / 739

页数：11

共 67 条

[1] STRUCTURE OF RHOMBOHEDRAL 2 ZINC INSULIN CRYSTALS [J].