1RLB

RETINOL BINDING PROTEIN COMPLEXED WITH TRANSTHYRETIN

Summary for 1RLB

• Entry DOI: 10.2210/pdb1rlb/pdb
• Descriptor: TRANSTHYRETIN, RETINOL BINDING PROTEIN, RETINOIC ACID (3 entities in total)
• Functional Keywords: complex (protein-protein), complex (protein-protein) complex, complex (protein/protein)
• Biological source: Homo sapiens (human); More
• Cellular location: Secreted: P02766 P02753
• Total number of polymer chains: 6
• Total formula weight: 95865.46

Authors

Monaco, H.L.,Rizzi, M.,Coda, A. (deposition date: 1995-02-20, release date: 1996-04-11, Last modification date: 2024-10-16)

Primary citation

Monaco, H.L.,Rizzi, M.,Coda, A.
Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein.
Science, 268:1039-1041, 1995

PubMed 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.

PubMed: 7754382

Experimental method

X-RAY DIFFRACTION (3.1 Å)