Cellular and Molecular Life Sciences CMLS

, Volume 58, Issue 10, pp 1491–1521

Transthyretin: a review from a structural perspective

Authors

  • J.A. Hamilton
    • Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, 635 Barnhill Drive Indianapolis, Indiana 462022 (USA), Fax: +1 317 274 4686, e-mail: jsteinra@iupui.edu
  • M.D. Benson
    • Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, 635 Barnhill Drive Indianapolis, Indiana 462022 (USA)

DOI: 10.1007/PL00000791

Cite this article as:
Hamilton, J. & Benson, M. CMLS, Cell. Mol. Life Sci. (2001) 58: 1491. doi:10.1007/PL00000791

Abstract.

Transthyretin (formerly called prealbumin) plays important physiological roles as a transporter of thyroxine and retinol-binding protein. X-ray structural studies have provided information on the active conformation of the protein and the site of binding of both ligands. Transthyretin is also one of the precursor proteins commonly found in amyloid deposits. Both wild-type and single-amino-acid-substituted variants have been identified in amyloid deposits, the variants being more amyloidogenic. Sequencing of the gene and the resulting production of a transgenic mouse model have resulted in progress toward solving the mechanism of amyloid formation and detecting the variant gene in individuals at risk.

Key words. Transthyretin; throxine; retinol; vitamin A; amyloid; structure.

Copyright information

© Birkhäuser Verlag, 2001