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
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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
Rask, L., Valtersson, C., Anundi, H., Kvist, S., Eriksson, U. G., Dallner, G., & Peterson, P. A. (1983) · Experimental Cell Research · doi:10.1016/0014-4827(83)90112-x · Cited by 49
Self-citationFormation and properties of retinylphosphate galactose.
Peterson, P. A., Rask, L., Helting, T. B., Östberg, L., & Fernstedt, Y. (1976) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)33211-8 · Cited by 45
Self-citationNewcomer, M. E., Liljas, A., Eriksson, U., Sundelin, J., Rask, L., & Peterson, P. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43402-3 · Cited by 32
Self-citationHase, J., Kobashi, K., Nakai, N., & Onosaka, S. (1976) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a131080 · Cited by 29
Crystallization of and preliminary X-ray data for the plasma retinol-binding protein.
Newcomer, M. E., Liljas, A., Sundelin, J., Rask, L., & Peterson, P. A. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42979-6 · Cited by 27
Self-citationRecent developments in the fat-soluble vitamins. Metabolism and function of vitamin A.
Ja, O. (1969) · PubMed · Cited by 13
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
Sorted by citations
Green, N. M. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)84259-j · Cited by 1,020
Protein Oligomerization In The Endoplasmic Reticulum
Hurtley, S. M., & Helenius, A. (1989) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.05.110189.001425 · Cited by 1,002
Interior and surface of monomeric proteins
Miller, S., Janin, J., Lesk, A. M., & Chothia, C. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90038-6 · Cited by 952
Huber, R., & Carrell, R. W. (1989) · Biochemistry · doi:10.1021/bi00449a001 · Cited by 883
Crystal Structure of Hemoprotein Domain of P450BM-3, a Prototype for Microsomal P450's
Ravichandran, K. G., Boddupalli, S. S., Hasermann, C. A., Peterson, J. A., & Deisenhofer, J. (1993) · Science · doi:10.1126/science.8342039 · Cited by 879
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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