This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1rlb
From Proteopedia
RETINOL BINDING PROTEIN COMPLEXED WITH TRANSTHYRETIN
Overview
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.
About this Structure
1RLB is a Protein complex structure of sequences from Gallus gallus and Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein., Monaco HL, Rizzi M, Coda A, Science. 1995 May 19;268(5213):1039-41. PMID:7754382 Page seeded by OCA on Sat May 3 07:38:17 2008
