C-Type Lectins
- PMID: 28876846
- Bookshelf ID: NBK453028
- DOI: 10.1101/glycobiology.3e.034
C-Type Lectins
Excerpt
C-type lectins (CTLs) are Ca++-dependent glycan-binding proteins (GBPs) that share primary and secondary structural homology in their carbohydrate-recognition domains (CRDs). The CRD of CTLs is more generally defined as the CTL domain (CTLD), because not all proteins with this domain bind either glycans or Ca++. CTLs include collectins, selectins, endocytic receptors, and proteoglycans, some of which are secreted and others are transmembrane proteins. They often oligomerize, which increases their avidity for multivalent ligands. CTLs differ significantly in the types of glycans that they recognize with high affinity. These proteins function as adhesion and signaling receptors in many pathways, including homeostasis and innate immunity, and are crucial in inflammatory responses and leukocyte and platelet trafficking.
Copyright 2015-2017 by The Consortium of Glycobiology Editors, La Jolla, California. All rights reserved.
Sections
- DISCOVERY OF C-TYPE LECTINS AND COMMON STRUCTURAL MOTIFS
- DIFFERENT SUBFAMILIES OF C-TYPE LECTINS
- THE ASHWELL–MORELL RECEPTOR
- OTHER ENDOCYTIC C-TYPE LECTINS
- THE COLLECTINS
- THE MYELOID C-TYPE LECTINS
- THE SELECTINS
- PROTEOGLYCANS WITH C-TYPE LECTIN DOMAINS
- OTHER PROTEINS WITH C-TYPE LECTIN DOMAINS
- ACKNOWLEDGMENTS
- FURTHER READING
References
-
- Ashwell G, Morell AG. 1974. The role of surface carbohydrates in the hepatic recognition and transport of circulating glycoproteins. Adv Enzymol Relat Areas Mol Biol 41: 99–128. - PubMed
-
- Rosen SD, Singer MS, Yednock TA, Stoolman LM. 1985. Involvement of sialic acid on endothelial cells in organ-specific lymphocyte recirculation. Science 228: 1005–1007. - PubMed
-
- Norgard-Sumnicht KE, Varki NM, Varki A. 1993. Calcium-dependent heparin-like ligands for L-selectin in nonlymphoid endothelial cells. Science 261: 480–483. - PubMed
Publication types
LinkOut - more resources
Full Text Sources