I-type Lectins
- PMID: 20301278
- Bookshelf ID: NBK1959
I-type Lectins
Excerpt
I-type lectins are glycan-binding proteins that belong to the immunoglobulin superfamily (IgSF), excluding antibodies and T-cell receptors. Bioinformatics analyses of mammalian genomes predict more than 500 proteins of the IgSF, other than antibodies and T-cell receptors. Thus, there is considerable potential for assignment to the I-type lectin family. In fact, the Siglec family of sialic acid–binding lectins is the only well-characterized group of I-type lectins, both structurally and functionally. These proteins are thus the major focus of this chapter. Details of their discovery, characterization, binding properties, and biology are provided, along with discussions of their functional implications in mammalian biology.
Copyright © 2009, The Consortium of Glycobiology Editors, La Jolla, California.
Sections
- HISTORICAL BACKGROUND AND OVERVIEW
- I-TYPE LECTINS OTHER THAN SIGLECS
- TWO MAJOR SUBFAMILIES OF SIGLECS
- COMMON FEATURES OF SIGLECS
- STRUCTURAL BASIS OF SIGLEC BINDING TO SIALYLATED GLYCANS
- EXPRESSION PATTERNS AND FUNCTIONS OF THE CONSERVED SIGLECS
- GENOMIC ORGANIZATION AND EVOLUTION OF CD33-RELATED SIGLECS
- STRUCTURE, EXPRESSION, AND FUNCTIONS OF CD33-RELATED SIGLECS
- NATURAL MUTATIONS OF THE “ESSENTIAL” ARGININE RESIDUE
- HUMAN-SPECIFIC CHANGES IN SIGLEC BIOLOGY
- FURTHER READING
References
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- Crocker PR, Varki A. Siglecs, sialic acids and innate immunity. Trends Immunol. 2001;22:337–342. - PubMed
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