Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 19 May 1995:
Vol. 268. no. 5213, pp. 1039 - 1041
DOI: 10.1126/science.7754382
Prev | Table of Contents | Next

Articles

Science, Vol 268, Issue 5213, 1039-1041
Copyright © 1995 by American Association for the Advancement of Science

articles

Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein

HL Monaco, M Rizzi, and A Coda

Department of Genetics, University of Pavia, Italy.

The three-dimensional structure of the complex formed by two plasma proteins, transthyretin and retinol-binding protein, was determined from x-ray diffraction data to a nominal resolution of 3.1 angstroms. One tetramer of transthyretin was bound to two molecules of retinol-binding protein. The two retinol-binding protein molecules established molecular interactions with the same transthyretin dimer, and each also made contacts with one of the other two monomers. Thus, the other two potential binding sites in a transthyretin tetramer were blocked. The amino acid residues of the retinol-binding protein that were involved in the contacts were close to the retinol-binding site.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Transthyretin levels in the vitreous correlate with change in visual acuity after vitrectomy.
E Van Aken, E A De Letter, M Veckeneer, L Derycke, T van Enschot, I Geers, S Delanghe, and J R Delanghe (2009)
Br J Ophthalmol 93, 1539-1545
   Abstract »    Full Text »    PDF »
Amyloidogenic Potential of Transthyretin Variants: INSIGHTS FROM STRUCTURAL AND COMPUTATIONAL ANALYSES.
L. Cendron, A. Trovato, F. Seno, C. Folli, B. Alfieri, G. Zanotti, and R. Berni (2009)
J. Biol. Chem. 284, 25832-25841
   Abstract »    Full Text »    PDF »
Identification and Characterization of a Non-retinoid Ligand for Retinol-binding Protein 4 Which Lowers Serum Retinol-binding Protein 4 Levels in Vivo.
A. Motani, Z. Wang, M. Conn, K. Siegler, Y. Zhang, Q. Liu, S. Johnstone, H. Xu, S. Thibault, Y. Wang, et al. (2009)
J. Biol. Chem. 284, 7673-7680
   Abstract »    Full Text »    PDF »
Decreased clearance of serum retinol-binding protein and elevated levels of transthyretin in insulin-resistant ob/ob mice.
N. Mody, T. E. Graham, Y. Tsuji, Q. Yang, and B. B. Kahn (2008)
Am J Physiol Endocrinol Metab 294, E785-E793
   Abstract »    Full Text »    PDF »
Different disease-causing mutations in transthyretin trigger the same conformational conversion.
R. E. Steward, R. S. Armen, and V. Daggett (2008)
Protein Eng. Des. Sel. 21, 187-195
   Abstract »    Full Text »    PDF »
Serum Retinol-Binding Protein 4 Concentration and Its Ratio to Serum Retinol Are Associated with Obesity and Metabolic Syndrome Components in Children.
I. Aeberli, R. Biebinger, R. Lehmann, D. l'Allemand, G. A. Spinas, and M. B. Zimmermann (2007)
J. Clin. Endocrinol. Metab. 92, 4359-4365
   Abstract »    Full Text »    PDF »
A Membrane Receptor for Retinol Binding Protein Mediates Cellular Uptake of Vitamin A.
R. Kawaguchi, J. Yu, J. Honda, J. Hu, J. Whitelegge, P. Ping, P. Wiita, D. Bok, and H. Sun (2007)
Science 315, 820-825
   Abstract »    Full Text »    PDF »
Odorant Binding and Conformational Dynamics in the Odorant-binding Protein.
E. Hajjar, D. Perahia, H. Debat, C. Nespoulous, and C. H. Robert (2006)
J. Biol. Chem. 281, 29929-29937
   Abstract »    Full Text »    PDF »
Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis.
N. S. Green, T. R. Foss, and J. W. Kelly (2005)
PNAS 102, 14545-14550
   Abstract »    Full Text »    PDF »
Pathways of Vitamin A Delivery to the Embryo: Insights from a New Tunable Model of Embryonic Vitamin A Deficiency.
L. Quadro, L. Hamberger, M. E. Gottesman, F. Wang, V. Colantuoni, W. S. Blaner, and C. L. Mendelsohn (2005)
Endocrinology 146, 4479-4490
   Abstract »    Full Text »    PDF »
The Crystal Structure of Transthyretin in Complex with Diethylstilbestrol: A PROMISING TEMPLATE FOR THE DESIGN OF AMYLOID INHIBITORS.
E. Morais-de-Sa, P. J. B. Pereira, M. J. Saraiva, and A. M. Damas (2004)
J. Biol. Chem. 279, 53483-53490
   Abstract »    Full Text »    PDF »
The role of extrahepatic retinol binding protein in the mobilization of retinoid stores.
L. Quadro, W. S. Blaner, L. Hamberger, P. M. Novikoff, S. Vogel, R. Piantedosi, M. E. Gottesman, and V. Colantuoni (2004)
J. Lipid Res. 45, 1975-1982
   Abstract »    Full Text »    PDF »
High Resolution Crystal Structures of Piscine Transthyretin Reveal Different Binding Modes for Triiodothyronine and Thyroxine.
T. Eneqvist, E. Lundberg, A. Karlsson, S. Huang, C. R. A. Santos, D. M. Power, and A. E. Sauer-Eriksson (2004)
J. Biol. Chem. 279, 26411-26416
   Abstract »    Full Text »    PDF »
Muscle Expression of Human Retinol-binding Protein (RBP). SUPPRESSION OF THE VISUAL DEFECT OF RBP KNOCKOUT MICE.
L. Quadro, W. S. Blaner, L. Hamberger, R. N. Van Gelder, S. Vogel, R. Piantedosi, P. Gouras, V. Colantuoni, and M. E. Gottesman (2002)
J. Biol. Chem. 277, 30191-30197
   Abstract »    Full Text »    PDF »
The V122I cardiomyopathy variant of transthyretin increases the velocity of rate-limiting tetramer dissociation, resulting in accelerated amyloidosis.
X. Jiang, J. N. Buxbaum, and J. W. Kelly (2001)
PNAS 98, 14943-14948
   Abstract »    Full Text »    PDF »
Capture of a Dimeric Intermediate during Transthyretin Amyloid Formation.
A. Olofsson, H. J. Ippel, V. Baranov, P. Horstedt, S. Wijmenga, and E. Lundgren (2001)
J. Biol. Chem. 276, 39592-39599
   Abstract »    Full Text »    PDF »
Ligand-Binding Proteins: Their Potential for Application in Systems for Controlled Delivery and Uptake of Ligands.
F. A. De Wolf and G. M. Brett (2000)
Pharmacol. Rev. 52, 207-236
   Abstract »    Full Text »    PDF »
Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold.
G. Beste, F. S. Schmidt, T. Stibora, and A. Skerra (1999)
PNAS 96, 1898-1903
   Abstract »    Full Text »    PDF »
Inhibiting transthyretin conformational changes that lead to amyloid fibril formation.
S. A. Peterson, T. Klabunde, H. A. Lashuel, H. Purkey, J. C. Sacchettini, and J. W. Kelly (1998)
PNAS 95, 12956-12960
   Abstract »    Full Text »    PDF »
The Crystal Structure of Amyloidogenic Leu55 right-arrow Pro Transthyretin Variant Reveals a Possible Pathway for Transthyretin Polymerization into Amyloid Fibrils.
M. P. Sebastiao, M. J. Saraiva, and A. M. Damas (1998)
J. Biol. Chem. 273, 24715-24722
   Abstract »    Full Text »    PDF »
Unique Biochemical Nature of Carp Retinol-binding Protein. N-LINKED GLYCOSYLATION AND UNCLEAVABLE NH2-TERMINAL SIGNAL PEPTIDE.
D. Bellovino, T. Morimoto, E. Mengheri, G. Perozzi, I. Garaguso, F. Nobili, and S. Gaetani (2001)
J. Biol. Chem. 276, 13949-13956
   Abstract »    Full Text »    PDF »
Synthesis of an Analog of the Thyroid Hormone-binding Protein Transthyretin via Regioselective Chemical Ligation.
J. A. Wilce, S. G. Love, S. J. Richardson, P. F. Alewood, and D. J. Craik (2001)
J. Biol. Chem. 276, 25997-26003
   Abstract »    Full Text »    PDF »
Support for the multigenic hypothesis of amyloidosis: The binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity invitro.
J. T. White and J. W. Kelly (2001)
PNAS 98, 13019-13024
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)