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Titolo:
Structural distribution of mutations associated with familial amyloidotic polyneuropathy in human transthyretin
Autore:
Eneqvist, T; Sauer-Eriksson, AE;
Indirizzi:
Umea Univ, Umea Ctr Mol Pathogenesis, SE-90187 Umea, Sweden Umea Univ Umea Sweden SE-90187 r Mol Pathogenesis, SE-90187 Umea, Sweden
Titolo Testata:
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
fascicolo: 3, volume: 8, anno: 2001,
pagine: 149 - 168
SICI:
1350-6129(200109)8:3<149:SDOMAW>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETINOL-BINDING PROTEIN; AMINO-ACID-SEQUENCE; THYROID-HORMONE-BINDING; SENILE SYSTEMIC AMYLOIDOSIS; GENE-EXPRESSION; CRYSTAL-STRUCTURE; T4 LYSOZYME; MAMMALIAN TRANSTHYRETIN; NUCLEOTIDE-SEQUENCE; RAT TRANSTHYRETIN;
Keywords:
amyloid; transthyretin; structure; familial amyloidotic polyneuropathy; evolution; beta-slip; thyroid hormone; retinol-binding protein;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
83
Recensione:
Indirizzi per estratti:
Indirizzo: Sauer-Eriksson, AE Umea Univ, Umea Ctr Mol Pathogenesis, SE-90187 Umea, Sweden Umea Univ Umea Sweden SE-90187 SE-90187 Umea, Sweden
Citazione:
T. Eneqvist e A.E. Sauer-Eriksson, "Structural distribution of mutations associated with familial amyloidotic polyneuropathy in human transthyretin", AMYLOID, 8(3), 2001, pp. 149-168

Abstract

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, 74point mutations are known to enhance amyloid formation causing familial amyloidotic polyneuropathy (FAP). Alignment of TTR sequences from twenty different species shows that only six of these mutations occur as natural aminoacids 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 08:56:57