2bfi
From Proteopedia
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(New page: 200px<br /><applet load="2bfi" size="350" color="white" frame="true" align="right" spinBox="true" caption="2bfi, resolution 1.1Å" /> '''MOLECULAR BASIS FOR A...)
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Revision as of 16:23, 29 January 2008
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MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY
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
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