TAILIEUCHUNG - Báo cáo khoa học: Structural disorder in amyloid fibrils: its implication in dynamic interactions of proteins

Proteins are occasionally converted from their normal soluble state to highly ordered fibrillar aggregates (amyloids), which give rise to pathologi-cal conditions that range from neurodegenerative disorders to systemic amyloidoses. Recent methodological advances in solid-state NMR and EPR spectroscopy have enabled determination of the 3D structure of sev-eral amyloids at residue-level resolution. | MINIREVIEW Structural disorder in amyloid fibrils its implication in dynamic interactions of proteins P. Tompa Institute of Enzymology BiologicalResearch Center Hungarian Academy of Sciences Budapest Hungary Keywords amyloid amyloid core disorder-to-order transition dynamic interaction fuzzy complex prion induced folding intrinsically disordered protein intrinsically unstructured protein polymorphism Correspondence P. Tompa Institute of Enzymology Biological Research Center Hungarian Academy of Sciences PO Box 7 H-1518 Budapest Hungary Fax 361 466 5465 Tel 361 279 3143 E-mail tompa@ Website http Received 22 May 2009 revised 24 July 2009 accepted 30 July 2009 doi Proteins are occasionally converted from their normal soluble state to highly ordered fibrillar aggregates amyloids which give rise to pathological conditions that range from neurodegenerative disorders to systemic amyloidoses. Recent methodological advances in solid-state NMR and EPR spectroscopy have enabled determination of the 3D structure of several amyloids at residue-level resolution. The general picture that emerges is that amyloids constitute parallel b sheets in which individual polypeptide chains run roughly perpendicular to the major axis of the fibril and are stacked in-register. Thus the unifying theme of amyloid formation is the structural transition from an initial globular or intrinsically disordered state to a highly ordered regular form. In this minireview we show that this description is somewhat oversimplified because part of the polypeptide chain in the amyloid remains intrinsically disordered and does not become part of the ordered core. As demonstrated through examples such as the amyloids of a-synuclein and Ab peptide and the yeast prions HET-s and Ure2p these disordered segments are depleted in amino acids NQFYV and are enriched in DEKP. They are also significantly more charged and have a higher predicted disordered value than

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