1G1O

CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETIN MUTANT TTR G53S/E54D/L55S

Summary for 1G1O

• Entry DOI: 10.2210/pdb1g1o/pdb
• Descriptor: TRANSTHYRETIN (2 entities in total)
• Functional Keywords: greek key, beta barrel, beta-slip, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02766
• Total number of polymer chains: 4
• Total formula weight: 55069.12

Authors

Eneqvist, T.,Andersson, K.,Olofsson, A.,Lundgren, E.,Sauer-Eriksson, A.E. (deposition date: 2000-10-13, release date: 2001-10-17, Last modification date: 2024-02-07)

Primary citation

Eneqvist, T.,Andersson, K.,Olofsson, A.,Lundgren, E.,Sauer-Eriksson, A.E.
The beta-slip: a novel concept in transthyretin amyloidosis.
Mol.Cell, 6:1207-1218, 2000

PubMed Abstract: Transthyretin is a tetrameric plasma protein associated with two forms of amyloid disease. The structure of the highly amyloidogenic transthyretin triple mutant TTRG53S/E54D/L55S determined at 2.3 A resolution reveals a novel conformation: the beta-slip. A three-residue shift in beta strand D places Leu-58 at the position normally occupied by Leu-55 now mutated to serine. The beta-slip is best defined in two of the four monomers, where it makes new protein-protein interactions to an area normally involved in complex formation with retinol-binding protein. This interaction creates unique packing arrangements, where two protein helices combine to form a double helix in agreement with fiber diffraction and electron microscopy data. Based on these findings, a novel model for transthyretin amyloid formation is presented.

PubMed: 11106758
DOI: 10.1016/S1097-2765(00)00117-9

Experimental method

X-RAY DIFFRACTION (2.3 Å)