- Introduction
- C. elegans proteins containing the CTLD motif have been compared to reveal their overall domain organization, to establish evolutionary relationships amongst the CTLDs and to determine the degree of conservation of amino acid residues that form Ca2+- and carbohydrate-binding sites in vertebrate C-type CRDs. The results raise the possibility that a small subset of these proteins have carbohydrate recognition functions analogous to those of vertebrate CRDs.
- A total of 183 CTLDs have been identified in 125 proteins encoded in the C. elegans genome. The CTLDs have been categorized into 8 evolutionary groups. The CTLD-containing proteins have been classified based on the overall arrangement of structural modules within the polypeptides, and on sequence similarity between the CTLDs. They also have a characteristic set of disulfide bonding patterns. The C. elegans proteins generally have different domain organization from known Drosophila melanogaster and mammalian proteins containing CTLDs. Most of the CTLDs are divergent in sequence from those in mammalian proteins. However, 19 show conservation of most of the amino acid residues that ligate Ca2+ to form a carbohydrate-binding site in vertebrate C-type CRDs.
- Domain organization of CTLD-containing proteins in C elegans
- CTLDs are coloured according to predicted sugar-binding specificity: blue, mannose; green, galactose; orange, N-acetylgalactosamine.
- Click on a protein architecture to view proteins in that family.
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For further information see:
Drickamer, K and Dodd, RB (1999) C-type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence. Glycobiology, 9, 1357-1369.
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