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A peptide from the adenovirus fiber shaft forms amyloid‐type fibrils
Author(s) -
Luckey Mary,
Hernandez Jean-François,
Arlaud Gérard,
Forsyth V.Trevor,
Ruigrok Rob W.H.,
Mitraki Anna
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01184-4
Subject(s) - fibril , peptide , fiber diffraction , fiber , amyloid (mycology) , biophysics , chemistry , electron microscope , crystallography , biochemistry , diffraction , x ray crystallography , biology , optics , physics , inorganic chemistry , organic chemistry
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 Å 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.