A peptide from the adenovirus fiber shaft forms amyloid-type fibrils

被引:31
作者
Luckey, M
Hernandez, JF
Arlaud, G
Forsyth, VT
Ruigrok, RWH
Mitraki, A
机构
[1] Inst Biol Struct, F-38027 Grenoble 1, France
[2] San Francisco State Univ, Dept Chem & Biochem, San Francisco, CA 94132 USA
[3] Univ Keele, Dept Phys, Keele ST5 5BG, Staffs, England
[4] Inst Max Von Laue Paul Langevin, Grenoble Outstn, European Mol Biol Lab, F-38042 Grenoble 9, France
关键词
adenovirus; amyloid fibril; electron microscopy; congo red; X-ray diffraction;
D O I
10.1016/S0014-5793(00)01184-4
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 fiber protein of adenovirus consists of a C-terminal globular head, a shaft and a short N-terminal tail. The crystal structure of a stable domain comprising the head plus a part of the shaft of human adenovirus type 2 fiber has recently been solved at 2.4 Angstrom resolution [van Raaij et al, (1999) Nature 401, 935-938], A peptide corresponding to the portion of the shaft immediately adjacent to the head (residues 355-396) has been synthesized chemically. The peptide failed to assemble correctly and instead formed amyloid-type fibrils as assessed by electron microscopy, Congo red binding and X-ray diffraction, Peptides corresponding to the fiber shaft could provide a model system to study mechanisms of amyloid fibril formation. (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:23 / 27
页数:5
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