Recent atomic models of amyloid fibril structure.
Despite the difficulties associated with determining atomic-level structures for materials that are fibrous, structural biologists are making headway in understanding the architecture of amyloid-like fibrils. It has long been recognized that these fibrils contain a cross-beta spine, with beta-strands perpendicular to the fibril axis. Recently, atomic structures have been determined for some of these cross-beta spines, revealing a pair of beta-sheets mated closely together by intermeshing sidechains in what has been termed a steric zipper. To explain the conversion of proteins from soluble to fibrous forms, several types of models have been proposed: refolding, natively disordered and gain of interaction. The gain-of-interaction models may additionally be subdivided into direct stacking, cross-beta spine, three-dimensional domain swapping and three-dimensional domain swapping with a cross-beta spine.
Howard Hughes Medical Institute, UCLA-DOE Institute for Genomics and Proteomics, Box 951570, UCLA, Los Angeles, CA 90095-1570, USA.
Rebecca
R
Nelson
David
D
Eisenberg
D000682:Amyloid / Q000737:chemistry*; D006860:Hydrogen Bonding; D008958:Models, Molecular; D011485:Protein Binding; D017510:Protein Folding
D000682:Amyloid