CTLDs in Drosophila melanogaster
- Introduction
- Drosophila melanogaster 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 33 CTLDs have been identified encoded in the D. melanogaster genome. The proteins have been classified based on the overall arrangement of modules within the polypeptides and based on sequence similarity between the CTLDs. The D. melanogaster proteins generally have different domain organization to known C. elegans and mammalian proteins containing CTLDs. Most of the CTLDs are divergent in sequence from those in mammalian proteins. However, 6 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 Drosophila melanogaster
- 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:
Dodd, RB and Drickamer, K (2001) Lectin-like proteins in model organisms: implications for evolution of carbohydrate-binding activity. Glycobiology 11, 71R-79R. PDF version.
