1F41

CRYSTAL STRUCTURE OF HUMAN TRANSTHYRETIN AT 1.5A RESOLUTION

Summary for 1F41

• Entry DOI: 10.2210/pdb1f41/pdb
• Descriptor: TRANSTHYRETIN (2 entities in total)
• Functional Keywords: greek key beta barrel, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02766
• Total number of polymer chains: 2
• Total formula weight: 27554.72

Authors

Hornberg, A.,Eneqvist, T.,Olofsson, A.,Lundgren, E.,Sauer-Eriksson, A.E. (deposition date: 2000-06-07, release date: 2000-09-20, Last modification date: 2024-02-07)

Primary citation

Hornberg, A.,Eneqvist, T.,Olofsson, A.,Lundgren, E.,Sauer-Eriksson, A.E.
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin.
J.Mol.Biol., 302:649-669, 2000

PubMed 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 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.

PubMed: 10986125
DOI: 10.1006/jmbi.2000.4078

Experimental method

X-RAY DIFFRACTION (1.3 Å)