Structural properties of an amyloid precursor of β2-microglobulin

被引：185

作者：

McParland, VJ ^{[1
]}

Kalverda, AP ^{[1
]}

Homans, SW ^{[1
]}

Radford, SE ^{[1
]}

机构：

[1] Univ Leeds, Sch Biochem & Mol Biol, Leeds LS2 9JT, W Yorkshire, England

来源：

NATURE STRUCTURAL BIOLOGY | 2002年 / 9卷 / 05期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1038/nsb791

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：

The population of one or more partially folded states has been proposed as a critical initial step in amyloid formation for several proteins. Here we use equilibrium denaturation measured by H-1-N-15 NMR to determine the conformational properties of an amyloidogenic intermediate of human beta(2)-microglobulin (beta(2)m) formed at low pH. The data show that this amyloid precursor is a noncooperatively stabilized ensemble that retains stable structure in five of the seven beta-strands that comprise the native fold. The amyloid precursors of beta(2)m and transthyretin have similar properties despite having structurally unrelated native folds. The data offer a rationale as to why these proteins are both amyloidogenic at low pH and suggest that amyloidosis of these and other proteins may involve ordered assembly from a precursor with similar conformational features.

引用

页码：326 / 331

页数：6

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