1f41
CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN AT 1.5A RESOLUTION
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OverviewOverview
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 not consistent 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 A 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.
DiseaseDisease
Known diseases associated with this structure: Amyloid neuropathy, familial, several allelic types OMIM:[176300], Amyloidosis, senile systemic OMIM:[176300], Carpal tunnel syndrome, familial OMIM:[176300], Dystransthyretinemic hyperthyroxinemia OMIM:[176300]
About this StructureAbout this Structure
1F41 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin., Hornberg A, Eneqvist T, Olofsson A, Lundgren E, Sauer-Eriksson AE, J Mol Biol. 2000 Sep 22;302(3):649-69. PMID:10986125
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