The DOI matches its Crossref record; 16 of the 17 references it cites were found in a registry or an index.
The three‐dimensional structure of retinol‐binding protein.
Open accessAbstract
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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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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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In the citing paper
“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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Citations
Cites
The Anatomy and Taxonomy of Protein Structure
Richardson, J. S. (1981) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60520-3 · Cited by 3,378
Blake, C. C. F., Geisow, M. J., Oatley, S. J., Rérat, B., & Rérat, C. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90368-6 · Cited by 792
Winkler, B. (2012) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767312099825 · Cited by 701
Structure of beef liver catalase
Murthy, M. R. N., Reid, T. J. A., Sicignano, A., Tanaka, N., & Rossmann, M. G. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90254-0 · Cited by 428
Orthogonal packing of .beta.-pleated sheets in proteins
Chothia, C., & Janin, J. (1982) · Biochemistry · doi:10.1021/bi00260a009 · Cited by 144
Demonstration in Serum of two Physiological Forms of the Human Retinol Binding Protein*
Peterson, P. A. (1971) · European Journal of Clinical Investigation · doi:10.1111/j.1365-2362.1971.tb00555.x · Cited by 98
Self-citationThe primary structure of the human retinol‐binding protein
Rask, L., Anundi, H., & Peterson, P. A. (1979) · FEBS Letters · doi:10.1016/0014-5793(79)81084-4 · Cited by 97
Self-citationRask, L., Anundi, H., Böhme, J., Eriksson, U., Fredriksson, A., Nilsson, S. F., Ronne, H., Vahlquist, A., & Peterson, P. A. (1980) · PubMed · Cited by 93
Self-citationSTRUCTURAL AND FUNCTIONAL STUDIES OF VITAMIN A‐BINDING PROTEINS*
Rask, L., Anundi, H., Böhme, J., Eriksson, U., Ronne, H., Sege, K., & Peterson, P. A. (1981) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1981.tb12739.x · Cited by 69
Self-citationShidoji, Y., & Muto, Y. (1977) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)41584-6 · Cited by 69
Research works printed but not linked: 2
- Moore,T. (1972) in Sebrell,W. and Harris,R.S. (eds.), The Vitamins, 1, Academic Press, NY, pp. 245-266.
- Olson,J.A. (1969) Fed. Proc., 28, 1670-1677.
Cited by
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Items 401–410 of 410
Åkerström, B. (2002) · Wiley eBooks · doi:10.1002/0471203076.emm0362
Fioroni, M., Dworeck, T., & Rodríguez-Ropero, F. (2013) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-7429-2_2
NMR Structures of Proteins Involved in Signal Transduction
Fesik, S. W., Meadows, R. P., Olejniczak, E. T., Petros, A. P., Hajduk, P. J., Yoon, H. S., Harlan, J. E., Logan, T. M., Zhou, M., Nettesheim, D. G., et al. (1996) · Springer eBooks · doi:10.1007/978-1-4613-0387-9_17
Adding bioactive compounds to wine and potential effects on health
Lagoutari, E., Lagoutari, M., Detsi, A., Zoumpoulakis, P. G., & Proestos, C. (2026) · Translational Food Sciences · doi:10.1093/trfood/vxag006
Structural and biochemical basis for retinol‐binding protein 4 antagonism by tinlarebant
Bassetto, M., & Kiser, P. D. (2026) · British Journal of Pharmacology · doi:10.1111/bph.70687
BindingDB Entry 50021299: Recent Advances on Small-Molecule Inhibitors of Lipocalin-like Proteins.
BindingDB (2025) · UC San Diego · doi:10.7270/q2x3533h
BindingDB (2022) · UC San Diego · doi:10.7270/q2251ntz
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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