TY - JOUR
T1 - A twisted four-sheeted model for an amyloid fibril
AU - Wang, Jimin
AU - Gülich, Susanne
AU - Bradford, Catharine
AU - Ramirez-Alvarado, Marina
AU - Regan, Lynne
N1 - Funding Information:
L.R. gratefully acknowledges the support of the National Institutes of Health (GM57265). J.W. acknowledges Yale University for the support of the directorship of the Center for Structural Biology. S.G. thanks Barry Piekos, Yale University for access to the TEM and for his advice in its use. We thank Aitziber López Cortajarena, Christopher Wilson, Irina Pozdnyakova, Janani Venkatraman, Thomas Magliery, Tommi Kajander, Simon Mochrie, and Peter Moore for discussions and thoughtful comments on the manuscript.
PY - 2005/9
Y1 - 2005/9
N2 - The formation of amyloid fibers and their deposition in the body is a characteristic of a number of devastating human diseases. Here, we propose a structural model, based on X-ray diffraction data, for the basic structure of an amyloid fibril formed by using the variants of the B1 domain of IgG binding protein G of Streptococcus. The model for the fibril incorporates four β sheets in a bundle with a diameter of 45 Å. Its cross-section, or layer, consists of four strands, one strand from each sheet. Layers stack on top of each other to form the fibril, which has an overall helical twist with a periodicity of about 154 Å. Each strand interacts in a parallel fashion with the strands in the layers above and below it, in an infinite β sheet. Some geometric features of this model and the logic behind it may be applicable for constructing other related cross-β amyloid fibrils.
AB - The formation of amyloid fibers and their deposition in the body is a characteristic of a number of devastating human diseases. Here, we propose a structural model, based on X-ray diffraction data, for the basic structure of an amyloid fibril formed by using the variants of the B1 domain of IgG binding protein G of Streptococcus. The model for the fibril incorporates four β sheets in a bundle with a diameter of 45 Å. Its cross-section, or layer, consists of four strands, one strand from each sheet. Layers stack on top of each other to form the fibril, which has an overall helical twist with a periodicity of about 154 Å. Each strand interacts in a parallel fashion with the strands in the layers above and below it, in an infinite β sheet. Some geometric features of this model and the logic behind it may be applicable for constructing other related cross-β amyloid fibrils.
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U2 - 10.1016/j.str.2005.06.010
DO - 10.1016/j.str.2005.06.010
M3 - Article
C2 - 16154085
AN - SCOPUS:24344498318
SN - 0969-2126
VL - 13
SP - 1279
EP - 1288
JO - Structure
JF - Structure
IS - 9
ER -