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Structural distribution of mutations associated with familial amyloidotic polyneuropathy in human transthyretin.
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
Umeå University, Faculty of Science and Technology, Umeå Centre for Molecular Pathogenesis (UCMP) (Faculty of Science and Technology).
2001 (English)In: Amyloid, ISSN 1350-6129, Vol. 8, no 3, 149-68 p.Article in journal (Refereed) Published
Abstract [en]

The human plasma protein transthyretin (TTR) is a highly stable soluble homotetrameric protein. Still, conformational changes in the wild type protein can lead to self-assembly into insoluble amyloid fibrils. In addition, 74 point mutations are known to enhance amyloid formation causing familial amyloidotic polyneuropathy (PAP). Alignment of TTR sequences from twenty different species shows that only six of these mutations occur as natural amino acids in other organisms. In this paper we analyse the distribution of FAP mutations within the three-dimensional structure of TTR. Contradictory to what might be expected from protein stability studies, the mutations are not restricted to structurally rigid parts of the molecule, nor are they concentrated at the monomer interaction sites.

Place, publisher, year, edition, pages
2001. Vol. 8, no 3, 149-68 p.
Keyword [en]
Amino Acid Sequence, Amyloid/*chemistry/genetics, Amyloid Neuropathies; Familial/*genetics, Animals, Binding Sites, Conserved Sequence, Evolution; Molecular, Hormones/metabolism, Humans, Models; Molecular, Molecular Sequence Data, Point Mutation, Prealbumin/chemistry/*genetics/metabolism, Protein Structure; Secondary, Retinol-Binding Proteins/metabolism, Surface Properties
Identifiers
URN: urn:nbn:se:umu:diva-13959PubMedID: 11676293OAI: oai:DiVA.org:umu-13959DiVA: diva2:153630
Available from: 2007-10-12 Created: 2007-10-12 Last updated: 2011-01-13Bibliographically approved

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Sauer-Eriksson, Elisabeth
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CiteExportLink to record
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