Structure of the epididymal retinoic acid binding protein at 2.1 Å resolution
Background: Androgen-dependent proteins in the lumen of the epididymis are required for sperm maturation. One of these is a retinoic acid binding protein, E-RABP, which binds both all-trans and 9-cis retinoic acid. The other retinoid-binding proteins whose structures are known do not bind 9-cis retinoids. Results: We describe the X-ray structure determination of E-RABP with and without bound ligand. The ligand binds deep in the β-barrel of the protein, the β-ionone ring innermost. The binding site, like the ligand, is amphipathic and the deepest part of the cavity is formed by a ring of aromatic amino acids. The isoprene tail of all-trans retinoic acid is bound in a folded conformation which resembles that of the 9-cis isomer. Conclusion: E-RABP achieves high-affinity binding of both all-trans and 9-cis isomers of retinoic acid by forcing the all-trans form to bind in a folded conformation. The RAR family of nuclear receptors for retinoic acid also binds both isomers, and their binding sites may therefore be similar. © 1993.
Publication Source (Journal or Book title)
Newcomer, M. (1993). Structure of the epididymal retinoic acid binding protein at 2.1 Å resolution. Structure, 1 (1), 7-18. https://doi.org/10.1016/0969-2126(93)90004-Z