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Titolo:
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin
Autore:
Hornberg, A; Eneqvist, T; Olofsson, A; Lundgren, E; Sauer-Eriksson, AE;
Indirizzi:
Umea Univ, Umea Ctr Mol Pathogenesis, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 Ctr Mol Pathogenesis, S-90187 Umea, Sweden Umea Univ, Dept Cell & Mol Biol, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 Dept Cell & Mol Biol, S-90187 Umea, Sweden
Titolo Testata:
JOURNAL OF MOLECULAR BIOLOGY
fascicolo: 3, volume: 302, anno: 2000,
pagine: 649 - 669
SICI:
0022-2836(20000922)302:3<649:ACAO2S>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
RETINOL-BINDING PROTEIN; X-RAY-DIFFRACTION; CRYSTAL-STRUCTURE DETERMINATION; HUMAN SERUM TRANSTHYRETIN; FIBRIL FORMATION; ALTERNATIVE CONFORMATIONS; MACROMOLECULAR STRUCTURES; VARIANT TRANSTHYRETIN; RESOLUTION; COMPLEX;
Keywords:
transthyretin; amyloidosis; X-ray structure; structural comparison; familial amyloidotic polyneuropathy;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
86
Recensione:
Indirizzi per estratti:
Indirizzo: Sauer-Eriksson, AE Umea Univ, Umea Ctr Mol Pathogenesis, S-90187 Umea, Sweden Umea Univ Umea Sweden S-90187 s, S-90187 Umea, Sweden
Citazione:
A. Hornberg et al., "A comparative analysis of 23 structures of the amyloidogenic protein transthyretin", J MOL BIOL, 302(3), 2000, pp. 649-669

Abstract

Self-assembly of the human plasma protein transthyretin (TTR) into unbranched insoluble amyloid fibrils occurs as a result of point mutations that destabilize the molecule, leading to conformational changes. The tertiary structure of native soluble TTR and many of its disease-causing mutants have been determined. Several independent studies by X-ray crystallography have suggested structural differences between TTR variants which are claimed to be of significance for amyloid formation. As these changes are minor and notconsistent between the studies, we have compared all TTR structures available at the protein data bank including three wild-types, three non-amyloidogenic mutants, seven amyloidogenic mutants and nine complexes. The reference for this study is a new 1.5 Angstrom resolution structure of human wild-type TTR refined to an R-factor/R-free of 18.6%/21.6%. The present findings are discussed in the light of the previous structural studies of TTR variants, and show the reported structural differences to be non-significant. (C)2000 Academic Press.

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Documento generato il 29/11/20 alle ore 02:50:03