2bfi
From Proteopedia
(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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==Overview== | ==Overview== | ||
- | The molecular structure of the amyloid fibril has remained elusive because | + | 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== | ==About this Structure== | ||
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[[Category: Atkins, E.]] | [[Category: Atkins, E.]] | ||
[[Category: Johansson, J.]] | [[Category: Johansson, J.]] | ||
- | [[Category: Makin, O | + | [[Category: Makin, O Sumner.]] |
- | [[Category: Serpell, L | + | [[Category: Serpell, L C.]] |
[[Category: Sikorski, P.]] | [[Category: Sikorski, P.]] | ||
[[Category: amyloid]] | [[Category: amyloid]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:37:18 2008'' |
Revision as of 14:37, 21 February 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
Page seeded by OCA on Thu Feb 21 16:37:18 2008