纤维
低温电子显微
化学
结晶学
电子显微镜
生物物理学
显微镜
淀粉样纤维
淀粉样蛋白(真菌学)
材料科学
淀粉样β
生物
医学
无机化学
物理
疾病
病理
光学
作者
Lothar Gremer,Daniel Schölzel,C. Schenk,Elke Reinartz,Jörg Labahn,Raimond B. G. Ravelli,Markus Tusche,Carmen López‐Iglesias,Wolfgang Hoyer,Henrike Heise,Dieter Willbold,Gunnar F. Schröder
出处
期刊:Science
[American Association for the Advancement of Science]
日期:2017-09-08
卷期号:358 (6359): 116-119
被引量:913
标识
DOI:10.1126/science.aao2825
摘要
Amyloids are implicated in neurodegenerative diseases. Fibrillar aggregates of the amyloid-β protein (Aβ) are the main component of the senile plaques found in brains of Alzheimer's disease patients. We present the structure of an Aβ(1-42) fibril composed of two intertwined protofilaments determined by cryo-electron microscopy (cryo-EM) to 4.0-angstrom resolution, complemented by solid-state nuclear magnetic resonance experiments. The backbone of all 42 residues and nearly all side chains are well resolved in the EM density map, including the entire N terminus, which is part of the cross-β structure resulting in an overall "LS"-shaped topology of individual subunits. The dimer interface protects the hydrophobic C termini from the solvent. The characteristic staggering of the nonplanar subunits results in markedly different fibril ends, termed "groove" and "ridge," leading to different binding pathways on both fibril ends, which has implications for fibril growth.
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