Transthyretin: a review from a structural perspective |
| |
Authors: | JA Hamilton MD Benson |
| |
Institution: | (1) 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, US;(2) Department of Pathology and Laboratory Medicine, Indiana University School of Medicine, 635 Barnhill Drive Indianapolis, Indiana 462022 (USA), US |
| |
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.
Received 23 January 2001; received after revision 4 April 2001; accepted 30 April 2001 |
| |
Keywords: | , Transthyretin, throxine, retinol, vitamin A, amyloid, structure, |
本文献已被 SpringerLink 等数据库收录! |
|