1g1o
From Proteopedia
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CRYSTAL STRUCTURE OF THE HIGHLY AMYLOIDOGENIC TRANSTHYRETIN MUTANT TTR G53S/E54D/L55S
Contents |
Overview
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.
Disease
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 Structure
1G1O is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The beta-slip: a novel concept in transthyretin amyloidosis., Eneqvist T, Andersson K, Olofsson A, Lundgren E, Sauer-Eriksson AE, Mol Cell. 2000 Nov;6(5):1207-18. PMID:11106758
Page seeded by OCA on Mon Nov 12 16:59:28 2007
