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 β-barrel) and by the conservation of a remarkable structural signature.
Original language | English |
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Pages (from-to) | 9-24 |
Number of pages | 16 |
Journal | BBA - Protein Structure and Molecular Enzymology |
Volume | 1482 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 18 Oct 2000 |
Keywords
- lipocalin
- fatty acid
- binding protein
- avidin
- structural comparison
- characteristic motif
- protein superfamily