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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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“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]
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“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]
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“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]
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“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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Sundelin, J., Das, S. R., Eriksson, U. J., Rask, L., & Peterson, P. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88999-2 · Cited by 123
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Self-citationBåvik, C., Eriksson, U., Allen, R. A., & Peterson, P. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98574-1 · Cited by 120
Self-citationThe interaction of retinol-binding protein with its plasma-membrane receptor.
Sivaprasadarao, A., & Findlay, J. B. C. (1988) · PubMed Central · Cited by 118
Structure in solution of a four‐helix lipid binding protein
Heinemann, B., Andersen, K. V., Nielsen, P. R., Bech, L. M., & Poulsen, F. M. (1996) · Protein Science · doi:10.1002/pro.5560050103 · Cited by 118
Harlan, J. E., Yoon, H. S., Hajduk, P. J., & Fesik, S. W. (1995) · Biochemistry · doi:10.1021/bi00031a006 · Cited by 118
Tsai, C., Lin, S. L., Wolfson, H. J., & Nussinov, R. (1996) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239609106582 · Cited by 117
Metadata
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › 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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