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The lipocalin protein family: structure and function

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FLOWER, Darren R.·1996·Biochemical Journal

DOI 10.1042/bj3180001PMC PMC1217580

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Abstract

The lipocalin protein family is a large group of small extracellular proteins. The family demonstrates great diversity at the sequence level; however, most lipocalins share three characteristic conserved sequence motifs, the kernel lipocalins, while a group of more divergent family members, the outlier lipocalins, share only one. Belying this sequence dissimilarity, lipocalin crystal structures are highly conserved and comprise a single eight-stranded continuously hydrogen-bonded antiparallel beta-barrel, which encloses an internal ligand-binding site. Together with two other families of ligand-binding proteins, the fatty-acid-binding proteins (FABPs) and the avidins, the lipocalins form part of an overall structural superfamily: the calycins. Members of the lipocalin family are characterized by several common molecular-recognition properties: the ability to bind a range of small hydrophobic molecules, binding to specific cell-surface receptors and the formation of complexes with soluble macromolecules. The varied biological functions of the lipocalins are mediated by one or more of these properties. In the past, the lipocalins have been classified as transport proteins; however, it is now clear that the lipocalins exhibit great functional diversity, with roles in retinol transport, invertebrate cryptic coloration, olfaction and pheromone transport, and prostaglandin synthesis. The lipocalins have also been implicated in the regulation of cell homoeostasis and the modulation of the immune response, and, as carrier proteins, to act in the general clearance of endogenous and exogenous compounds.

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Comprehensive insect physiology, biochemistry and pharmacology
Brooks, G. T. (1985) · Insect Biochemistry · doi:10.1016/0020-1790(85)90131-3 · Cited by 1,595
Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
Kjeldsen, L., Johnsen, A., Sengeløv, H., & Borregaard, N. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82217-7 · Cited by 1,286
The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
Papiz, M. Z., Sawyer, L., Eliopoulos, E., North, A. C. T., Findlay, J. B. C., Sivaprasadarao, A., Jones, T. A., Newcomer, M. E., & Kraulis, P. J. (1986) · Nature · doi:10.1038/324383a0 · Cited by 873
Transport and Storage of Vitamin A
Blomhoff, R., Green, M. H., Berg, T., & Norum, K. R. (1990) · Science · doi:10.1126/science.2218545 · Cited by 609
Drug binding to human alpha-1-acid glycoprotein in health and disease.
Kremer, J. M., Wilting, J., & Janssen, L. H. M. (1988) · Pharmacological Reviews · doi:10.1016/s0031-6997(25)00015-8 · Cited by 584
Advanced Dairy Chemistry
McSweeney, P. L. H., & Fox, P. F. (2013) · Springer eBooks · doi:10.1007/978-1-4614-4714-6 · Cited by 502
Structure of a complex of two plasma proteins: transthyretin and retinol-binding protein
Monaco, H. L., Rizzi, M., & Coda, A. (1995) · Science · doi:10.1126/science.7754382 · Cited by 413
Binding Affinities of Retinol and Related Compounds to Retinol Binding Proteins
Cogan, U., Kopelman, M., Mokady, S., & Shinitzky, M. (1976) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1976.tb10390.x · Cited by 381
Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography
Böcskei, Z., Groom, C. R., Flower, D. R., Wright, C. E., Phillips, S. E. V., Cavaggioni, A., Findlay, J. B. C., & North, A. C. T. (1992) · Nature · doi:10.1038/360186a0 · Cited by 361
Structure and sequence relationships in the lipocalins and related proteins
Flower, D. R., North, A. C. T., & Attwood, T. K. (1993) · Protein Science · doi:10.1002/pro.5560020507 · Cited by 342

Show all 148 references

Research works printed but not linked: 9

Sivaprasadarao, A., Boudjelal, M. and Findlay, J. B. C. (1993) Biochem. Soc. Trans. 21, 619-622
Goodman, W.S (1984) in The Retinoids (Sporn, M. B., Roberts, A. B. and Goodman, W. S, eds.), vol. 2, pp. 41-88, Academic Press, New York 40
Magert, H.-J., Hadrys, T., Cieslak, A., Groger, A., Feller, S. and Forssmann, W.-G. (1995) Proc. Natl. Acad. Sci. U.S.A. 92, 2091-2095
Pevsner, J., Trifiletti, R. R., Strittmatter, S. M. and Snyder, S. H. (1985) Proc. Natl. Acad. Sci. U.S.A. 82, 3050-3054
Nagata, A., Suzuki, Y., Igarashi, M., Eguchi, N., Toh, H., Urade, Y. and Hayaishi, O. (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 4020-4024
Julkunen, M., Seppala, M. and Janne, O. A. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 8845-8849 92
Mendez, E., Fernandez-Luna, J. L., Grubb, A. and Levy-Cobian (1986) Proc. Natl.Acad. Sci. U.S.A. 83, 3050-3054 101
Bennett, M. and Schmid, K. (1980) Proc. Natl. Acad. Sci. U.S.A. 77, 6109-6113 109
Spence, A. M., Sheppard, P. C., Davie, J. R., Matuo, Y., Nishi, N., McKeehan, W. L., Dodd, J. G. and Matusik, R. J. (1989) Proc. Natl. Acad. Sci. U.S.A. 86, 7843-7847 130

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Authors: FLOWER, D. R.
Affiliations: Department of Physical Chemistry and BioAnalysis, Astra Charnwood, Bakewell Road, Loughborough, Leics. LE11 5RH, U.K.
Corresponding author: FLOWER, Darren R.
ORCID: FLOWER, Darren R.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1996-08-15
Volume: 318
Issue: 1
Pages: 1-14
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3180001
PMC: PMC1217580
OpenAlex: W2040141270
Cited by: 1,679
References: 148
Citations by year: 2026: 24 · 2025: 33 · 2024: 41 · 2023: 53 · 2022: 49 · 2021: 64 · 2020: 68 · 2019: 51 · 2018: 43 · 2017: 53 · 2016: 69 · 2015: 73 · 2014: 79 · 2013: 81 · 2012: 91
FWCI: 3.93
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Interaction Studies and Fluorescence Analysis
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: lipocalin, protein structure, beta-barrel, ligand-binding proteins, fatty acid binding protein, avidin, retinol transport, cryptic coloration, olfaction, prostaglandin synthesis, cell surface receptors, membrane transporters, immune regulation
MeSH terms: Adjuvants, Immunologic, Amino Acid Sequence, Avidin, Carrier Proteins, Ligands, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Pheromones, Protein Binding, Proteins, Receptors, Cell Surface, Smell, Myelin P2 Protein, Fatty Acid-Binding Proteins

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The lipocalin protein family: structure and function

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