Article
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin.
Journal of molecular biology - 22 Sept 2000
Hörnberg A, Eneqvist T, Olofsson A, Lundgren E, Sauer-Eriksson A E
Abstract excerpt
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...
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