The three‐dimensional structure of retinol‐binding protein.
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The complex of retinol with its carrier protein, retinol-binding protein (RBP) has been crystallized and its three-dimensional structure determined using X-ray crystallography. Its most striking feature is an eight-stranded up-and-down beta barrel core that completely encapsulates the retinol molecule. The retinol molecule lies along the axis of the barrel with the beta-ionone ring innermost and the tip of the isoprene tail close to the surface.
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Retinol orientation in the CRBP pocket is reversed relative to holo-RBP4, with β-ionone near the pocket mouth and the hydroxyl group hydrogen bonding to a Glu residue at the cavity base.
“However, the orientation of retinol in the binding pocket is reversed in relation to that in holo-RBP4 with the β-ionone nearest the mouth of the pocket and the hydroxyl group hydrogen bonding with a Glu residue at the base of the cavity.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
The Results and Discussion (page unavailable) place the β-ionone ring deepest in RBP’s pocket and the isoprene tail near the protein surface, supporting the RBP side of the comparison. The paper does not describe retinol’s orientation in CRBP or a hydroxyl-group hydrogen bond to Glu at the cavity base. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAll-trans-retinol is oriented in the RBP4 binding pocket with its hydroxyl group facing solvent and its retinyl moiety bound by nonpolar residues, explaining high specificity for the all-trans isomer.
“all-trans-Retinol is oriented in the binding pocket with its hydroxyl group facing the solvent and the retinyl moiety snuggly bound by a number of nonpolar residues in a highly complementary fashion, explaining the high binding specificity toward the all-trans isomer.”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
The Results and Discussion describe all-trans-retinol in a complementary pocket lined by hydrophobic or uncharged residues, with its ionone ring deepest and its tail extending toward the protein surface. But they say retinol is essentially inaccessible to water, not that its hydroxyl group faces solvent. They also do not establish high specificity for the all-trans isomer; instead, they note that RBP may bind various retinyl derivatives. (LLM, conf=0.88)
Experimental — accuracy not yet measuredCRBP has a β-barrel fold that houses the retinoid-binding site.
“The structure of CRBP, similar to that of RBP4, features a β-barrel fold that houses the retinoid-binding site.495”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
The Results and Discussion describe a β-barrel with retinol inside it for RBP, supporting the comparison protein’s structure. But the same section says the structure of cRBP had yet to be elucidated; it does not establish that cRBP has that fold or binding-site arrangement. Page numbers are unavailable in our copy. (LLM, conf=0.88)
Experimental — accuracy not yet measuredHolo-RBP4 has an eight-stranded β-barrel core containing a single retinol-binding site.
“The main structural feature of holo-RBP4, determined crystallographically in the early 1980s, is an eight-stranded β-barrel core containing a single retinol-binding site (Figure 32).495”
From Chemistry of the Retinoid (Visual) Cycle (2014) · cites this paper as [495]
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- Authors
- Newcomer, M. E., Jones, T. A., Aqvist, J., Sundelin, J., Eriksson, U., Rask, L., & Peterson, P. A.
- Affiliations
- Uppsala University (SE)
- Venue
- The EMBO Journal
- Published
- 1984-07-01
- Volume
- 3
- Issue
- 7
- Pages
- 1451-1454
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC557543
- OpenAlex
- W1221193043
- Cited by
- 405
- References
- 17
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 4 · 2023: 1 · 2022: 2 · 2021: 4 · 2020: 5 · 2019: 1 · 2016: 3 · 2015: 5 · 2014: 8 · 2013: 9 · 2012: 3
- FWCI
- 19.55
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The EMBO Journal (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Civil War Book Review (submittedVersion)
- Funders
- National Institutes of Health
- Topics
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Retinoids in leukemia and cellular processes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- retinol-binding protein, retinol, vitamin A, protein structure, beta-barrel, protein-ligand complex, beta-ionone ring, crystal structure
- MeSH terms
- Animals, Binding Sites, Humans, Models, Molecular, Protein Conformation, Rabbits, Retinol-Binding Proteins, Vitamin A, X-Ray Diffraction, Rats
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