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Genomic analysis of C-type lectins.
Kurt Drickamer1, Andrew J Fadden
1Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OXI 3QU, U.K. kd@glycob.ox.ac.uk
Biochemical Society Symposium
|March 27, 2003
Summary
Lectins, proteins recognizing complex carbohydrates, play roles in immunity and cell signaling. Genome-wide analysis reveals diverse lectin families across species, aiding in understanding human lectin functions.
Area of Science:
- Biochemistry
- Molecular Biology
- Evolutionary Biology
Background:
- Complex carbohydrates mediate biological effects via lectins with carbohydrate-recognition domains.
- Seven distinct lectin families are involved in crucial cellular processes like trafficking, adhesion, signaling, and immunity.
- Genome-wide analysis enables comprehensive study of carbohydrate-binding domains.
Purpose of the Study:
- To propose an overall picture of lectins present in humans.
- To suggest ligand-binding activity for novel C-type lectin-like domains.
- To provide a basis for proposing potential biological functions of identified lectin domains.
Main Methods:
- Genome-wide analysis of potential carbohydrate-binding domains.
- Comparative analysis of lectin classes across species (yeast, invertebrates, vertebrates).
- Structural knowledge of C-type carbohydrate-recognition domains to infer function.
Main Results:
- Two intracellular lectin classes are conserved across yeast and vertebrates; two others are vertebrate-specific.
- Cell-surface lectins (C-type, galectins) are found in invertebrates and vertebrates, while I-type lectins are vertebrate-specific.
- Novel C-type lectin-like domains were identified in a human genome screen.
Conclusions:
- The evolutionary emergence of lectin classes correlates with oligosaccharide complexity.
- Ligand-binding activities can be proposed for novel C-type lectin-like domains based on structural similarities.
- Sequence analysis of proteins with these domains can predict their biological functions.