Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein.
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.
Monaco
H L
HL
Department of Genetics, University of Pavia, Italy.
Rizzi
M
M
Coda
A
A
D000595:Amino Acid Sequence; D000818:Animals; D001704:Biopolymers; D002645:Chickens; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011228:Prealbumin / Q000737:chemistry*; D011485:Protein Binding; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012177:Retinol-Binding Proteins / Q000737:chemistry*; D054839:Retinol-Binding Proteins, Plasma; D017386:Sequence Homology, Amino Acid
D001704:Biopolymers; D011228:Prealbumin; D012177:Retinol-Binding Proteins; D054839:Retinol-Binding Proteins, Plasma