2bfi: Difference between revisions
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[[Image:2bfi.gif|left|200px]] | [[Image:2bfi.gif|left|200px]] | ||
'''MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY''' | {{Structure | ||
|PDB= 2bfi |SIZE=350|CAPTION= <scene name='initialview01'>2bfi</scene>, resolution 1.1Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= | |||
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'''MOLECULAR BASIS FOR AMYLOID FIBRIL FORMATION AND STABILITY''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BFI is a [ | 2BFI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BFI OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15630094 15630094] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Atkins, E.]] | [[Category: Atkins, E.]] | ||
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[[Category: Sikorski, P.]] | [[Category: Sikorski, P.]] | ||
[[Category: amyloid]] | [[Category: amyloid]] | ||
[[Category: beta-sheet | [[Category: beta-sheet interaction]] | ||
[[Category: electron diffraction]] | [[Category: electron diffraction]] | ||
[[Category: fiber diffraction]] | [[Category: fiber diffraction]] | ||
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[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:01:17 2008'' | ||
Revision as of 14:01, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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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