Related Experiment Video
Updated: Aug 5, 2026

Real-time Analyses of Retinol Transport by the Membrane Receptor of Plasma Retinol Binding Protein
Published on: January 28, 2013
Three-dimensional structure of the transthyretin-retinol-binding protein complex
1Department of Science and Technology, Biocrystallography Laboratory, University of Verona, Verona, Italy. monaco@sci.univr.it
Abstract:
Transthyretin (TTR), formerly called prealbumin, one of the transporters of the hormone thyroxine and retinol-binding protein (RBP), the specific carrier of vitamin A, forms, under physiological conditions, a macromolecular complex that prevents glomerular filtration of the low-molecular-weight RBP in the kidneys. This paper describes briefly the three-dimensional structure of the two proteins as determined by X-ray diffraction analysis of single crystals and that of the complex that the two molecules form in plasma and discusses the non-crystallographic evidence that supports the model of the macromolecular complex.
More Related Videos
16:02Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation
Published on: February 10, 2023
07:22The Development and Application of Biophysical Assays for Evaluating Ternary Complex Formation Induced by Proteolysis Targeting Chimeras (PROTACS)
Published on: January 12, 2024
Related Concept Videos
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme can...
ATP Synthase: Structure
Protein Organization
The primary structure of a protein is its amino acid sequence.
Protein Translocation Machinery on the ER Membrane
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Electron Transport Chain: Complex III and IV
Structure of Porins