1g1o

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Revision as of 14:53, 12 November 2007

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spinqualitylabelsall models 1g1o, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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

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