Transthyretin

A review from a structural perspective

J. A. Hamilton, Merrill Benson

Research output: Contribution to journalArticle

162 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)1491-1521
Number of pages31
JournalCellular and Molecular Life Sciences
Volume58
Issue number10
StatePublished - 2001

Fingerprint

Prealbumin
Amyloid
Amyloid Plaques
Thyroxine-Binding Proteins
Deposits
Genes
Retinol-Binding Proteins
Protein Precursors
Protein Binding
Transgenic Mice
Conformations
Binding Sites
X-Rays
Ligands
Amino Acids
X rays
Proteins

Keywords

  • Amyloid
  • Retinol
  • Structure
  • Throxine
  • Transthyretin
  • Vitamin A

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Cell Biology

Cite this

Transthyretin : A review from a structural perspective. / Hamilton, J. A.; Benson, Merrill.

In: Cellular and Molecular Life Sciences, Vol. 58, No. 10, 2001, p. 1491-1521.

Research output: Contribution to journalArticle

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