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The beta-slip: a novel concept in transthyretin amyloidosis.
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
Faculty of Medicine, Molecular Biology (Faculty of Medicine). (Lundgren)
Faculty of Medicine, Molecular Biology (Faculty of Medicine). (Lundgren)
Faculty of Medicine, Molecular Biology (Faculty of Medicine). (Lundgren)
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2000 (English)In: Mol Cell, ISSN 1097-2765, Vol. 6, no 5, 1207-18 p.Article in journal (Refereed) Published
Abstract [en]

Transthyretin is a tetrameric plasma protein associated with two forms of amyloid disease. The structure of the highly amyloidogenic transthyretin triple mutant TTRG53S/E54D/L55S determined at 2.3 A resolution reveals a novel conformation: the beta-slip. A three-residue shift in beta strand D places Leu-58 at the position normally occupied by Leu-55 now mutated to serine. The beta-slip is best defined in two of the four monomers, where it makes new protein-protein interactions to an area normally involved in complex formation with retinol-binding protein. This interaction creates unique packing arrangements, where two protein helices combine to form a double helix in agreement with fiber diffraction and electron microscopy data. Based on these findings, a novel model for transthyretin amyloid formation is presented.

Place, publisher, year, edition, pages
2000. Vol. 6, no 5, 1207-18 p.
Keyword [en]
Amino Acid Substitution/genetics, Amyloidosis/genetics/*metabolism, Binding Sites, Crystallography; X-Ray, Epitopes/chemistry/metabolism, Humans, Hydrogen Bonding, Microscopy; Electron, Models; Biological, Models; Molecular, Mutation/genetics, Prealbumin/*chemistry/genetics/*metabolism, Protein Binding, Protein Folding, Protein Interaction Mapping, Protein Structure; Quaternary, Protein Structure; Secondary
Identifiers
URN: urn:nbn:se:umu:diva-13962PubMedID: 11106758OAI: oai:DiVA.org:umu-13962DiVA: diva2:153633
Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2011-01-14Bibliographically approved

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PubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=11106758&dopt=Citation

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Olofsson, AndersLundgren, ErikSauer-Eriksson, Elisabeth

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