2bfi | pdb_00002bfi
MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY
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Overview
The molecular structure of the amyloid fibril has remained elusive because, of the difficulty of growing well diffracting crystals. By using a, sequence-designed polypeptide, we have produced crystals of an amyloid, fiber. These crystals diffract to high resolution (1 A) by electron and, x-ray diffraction, enabling us to determine a detailed structure for, amyloid. The structure reveals that the polypeptides form fibrous crystals, composed of antiparallel beta-sheets in a cross-beta arrangement, characteristic of all amyloid fibers, and allows us to determine the, side-chain packing within an amyloid fiber. The antiparallel beta-sheets, are zipped together by means of pi-bonding between adjacent phenylalanine, rings and salt-bridges between charge pairs (glutamic acid-lysine), thus, controlling and stabilizing the structure. These interactions are likely, to be important in the formation and stability of other amyloid fibrils.
About this Structure
2BFI is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Molecular basis for amyloid fibril formation and stability., Makin OS, Atkins E, Sikorski P, Johansson J, Serpell LC, Proc Natl Acad Sci U S A. 2005 Jan 11;102(2):315-20. Epub 2005 Jan 3. PMID:15630094
Page seeded by OCA on Tue Jan 29 18:23:16 2008
