Transthyretin: a review from a structural perspective

Cell Mol Life Sci. 2001 Sep;58(10):1491-521. 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.

Publication types

  • Review

MeSH terms

  • Animals
  • Biological Transport
  • Crystallography, X-Ray
  • Genetic Variation
  • Humans
  • Ligands
  • Mice
  • Mice, Transgenic
  • Models, Molecular
  • Prealbumin / chemistry*
  • Prealbumin / genetics*
  • Prealbumin / metabolism
  • Prealbumin / physiology*
  • Protein Binding
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Thyroxine / metabolism

Substances

  • Ligands
  • Prealbumin
  • Recombinant Proteins
  • Thyroxine