Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein
- PMID: 7754382
- DOI: 10.1126/science.7754382
Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein
Abstract
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.
Similar articles
-
Three-dimensional structure of the transthyretin-retinol-binding protein complex.Clin Chem Lab Med. 2002 Dec;40(12):1229-36. doi: 10.1515/CCLM.2002.213. Clin Chem Lab Med. 2002. PMID: 12553423
-
Crystallization of the macromolecular complex transthyretin-retinol-binding protein.J Mol Biol. 1994 Nov 18;244(1):110-3. doi: 10.1006/jmbi.1994.1708. J Mol Biol. 1994. PMID: 7966314
-
Structural and mutational analyses of protein-protein interactions between transthyretin and retinol-binding protein.FEBS J. 2008 Dec;275(23):5841-54. doi: 10.1111/j.1742-4658.2008.06705.x. FEBS J. 2008. PMID: 19021760
-
Plasma retinol-binding protein: structure and interactions with retinol, retinoids, and transthyretin.Vitam Horm. 2004;69:271-95. doi: 10.1016/S0083-6729(04)69010-8. Vitam Horm. 2004. PMID: 15196886 Review.
-
Hepatic synthesis, maturation and complex formation between retinol-binding protein and transthyretin.Clin Chem Lab Med. 2002 Dec;40(12):1211-20. doi: 10.1515/CCLM.2002.211. Clin Chem Lab Med. 2002. PMID: 12553421 Review.
Cited by
-
Antibody interfaces revealed through structural mining.Comput Struct Biotechnol J. 2022 Aug 31;20:4952-4968. doi: 10.1016/j.csbj.2022.08.048. eCollection 2022. Comput Struct Biotechnol J. 2022. PMID: 36147680 Free PMC article.
-
Retinol-binding protein 4 as a risk factor for cholesterol gallstone formation.Mol Cell Biochem. 2013 May;377(1-2):219-27. doi: 10.1007/s11010-013-1587-9. Epub 2013 Feb 19. Mol Cell Biochem. 2013. PMID: 23420326
-
Inhibitors of Transthyretin Amyloidosis: How to Rank Drug Candidates Using X-ray Crystallography Data.Molecules. 2024 Feb 18;29(4):895. doi: 10.3390/molecules29040895. Molecules. 2024. PMID: 38398647 Free PMC article.
-
A molecular basis for tetramer destabilization and aggregation of transthyretin Ala97Ser.Protein Sci. 2023 Apr;32(4):e4610. doi: 10.1002/pro.4610. Protein Sci. 2023. PMID: 36851846 Free PMC article.
-
Support for the multigenic hypothesis of amyloidosis: the binding stoichiometry of retinol-binding protein, vitamin A, and thyroid hormone influences transthyretin amyloidogenicity in vitro.Proc Natl Acad Sci U S A. 2001 Nov 6;98(23):13019-24. doi: 10.1073/pnas.241406698. Epub 2001 Oct 30. Proc Natl Acad Sci U S A. 2001. PMID: 11687657 Free PMC article.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials