2BFI

Molecular basis for amyloid fibril formation and stability

Summary for 2BFI

• Entry DOI: 10.2210/pdb2bfi/pdb
• Descriptor: SYNTHETIC PEPTIDE (1 entity in total)
• Functional Keywords: amyloid, pi-pi bonding, beta-sheet interactions
• Biological source: SYNTHETIC CONSTRUCT
• Total number of polymer chains: 1
• Total formula weight: 1465.71

Authors

Makin, O.S.,Atkins, E.,Sikorski, P.,Johansson, J.,Serpell, L.C. (deposition date: 2004-12-07, release date: 2005-01-06, Last modification date: 2024-05-08)

Primary citation

Sumner Makin, O.,Atkins, E.,Sikorski, P.,Johansson, J.,Serpell, L.C.
Molecular Basis for Amyloid Fibril Formation and Stability
Proc.Natl.Acad.Sci.USA, 102:315-, 2005

PubMed Abstract: 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.

PubMed: 15630094
DOI: 10.1073/PNAS.0406847102

Experimental method

X-RAY DIFFRACTION (1.1 Å)