The lipocalin protein family: structural and sequence overview
Abstract
Lipocalins are remarkably diverse at the sequence level yet have highly conserved structures. Most lipocalins share three characteristic conserved sequence motifs - the kernel lipocalins - while others are more divergent family members - the outlier lipocalins - typically sharing only one or two. This classification is a useful tool for analysing the family, and within these large sets are smaller groups sharing much higher levels of sequence similarity. The lipocalins are also part of a larger protein superfamily: the calycins, which includes the fatty acid binding proteins, avidins, a group of metalloproteinase inhibitors, and triabin. The superfamily is characterised by a similar structure (a repeated +1 topology beta-barrel) and by the conservation of a remarkable structural signature.
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The ADAM and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions, and are involved in a range of human diseases.
“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [20]
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- Authors
- Flower, D. R., North, A. C. T., & Sansom, C. E.
- Affiliations
- Jenner Institute (GB)
- University of Leeds (GB)
- University of London (GB)
- Corresponding author
- Flower, Darren R.
- ORCID
- Flower, Darren R.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 2000-10
- Volume
- 1482
- Issue
- 1-2
- Pages
- 9-24
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W2038438679
- Cited by
- 868
- References
- 59
- Citations by year
- 2026: 18 · 2025: 26 · 2024: 25 · 2023: 27 · 2022: 29 · 2021: 33 · 2020: 37 · 2019: 27 · 2018: 29 · 2017: 35 · 2016: 46 · 2015: 39 · 2014: 51 · 2013: 37 · 2012: 60
- FWCI
- 1.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology (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
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- lipocalin, protein superfamilies, conserved motifs, fatty acid binding protein, avidin, metalloproteinase inhibitors, protein structure conservation
- MeSH terms
- Fatty Acid-Binding Protein 7, Amino Acid Sequence, Animals, Carrier Proteins, Humans, Lactoglobulins, Models, Molecular, Molecular Sequence Data, Neoplasm Proteins, Protein Conformation, Sequence Homology, Amino Acid, Insect Proteins, Tumor Suppressor Proteins, Fatty Acid-Binding Proteins
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