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, 2014 C-type lectins belong to a superfamily of receptors that share structural homology in their carbohydrate recognition domains and often bind to carbohydrates in a Ca-dependent fashion. Whereas endocytic C-type lectin receptors (CLRs) trigger the receptor-mediated endocytosis of soluble ligands, myeloid CLRs in innate immunity act as pattern recognition ...
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C-Type Lectin Receptors in Phagocytosis
2020C-type lectin receptors (CLRs) are a family of transmembrane proteins having at least one C-type lectin-like domain (CTLD) on the cell surface and either a short intracellular signaling tail or a transmembrane domain that facilitates interaction with a second protein, often the Fc receptor common gamma chain (FcRγ), that mediates signaling.
Kai Li, David M. Underhill
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Genomic analysis of C-type lectins
Biochemical Society Symposia, 2002Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate ...
Andrew J. Fadden, Kurt Drickamer
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A C-type lectin with antibacterial activity in weather loach, Misgurnus anguillicaudatus.
Journal of Fish Diseases, 2020C-type lectins are carbohydrate-binding proteins that play important roles in immunity by serving as pattern recognition receptors. In the present study, a novel nattectin-like C-type lectin was obtained from the weather loach, Misgurnus anguillicaudatus,
Xiao-Wen Zhang +6 more
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C-type Lectins in Immunity to Lung Pathogens
2020The respiratory tract is tasked with responding to a constant and vast influx of foreign agents. It acts as an important first line of defense in the innate immune system and as such plays a crucial role in preventing the entry of invading pathogens.
Raymond, Benjamin +2 more
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Myeloid C-type lectins in innate immunity
Nature Immunology, 2006C-type lectins expressed on myeloid cells comprise a family of proteins that share a common structural motif, and some act as receptors in pathogen recognition. But just as the presence of leucine-rich repeats alone is not sufficient to define a Toll-like receptor, the characterization of C-type lectin receptors in innate immunity requires the ...
Robinson, Matthew J +4 more
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2012
Historically the C-Type lectins (CLEC) or C-type lectin receptors (CLR) form a family of Ca2+ dependent carbohydrate binding proteins which have a common sequence motif of 115–130 amino acid residues, referred to as the carbohydrate recognition domain (CRD). The C-type designation is from their requirement for calcium for binding.
Anita Gupta, G. S. Gupta
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Historically the C-Type lectins (CLEC) or C-type lectin receptors (CLR) form a family of Ca2+ dependent carbohydrate binding proteins which have a common sequence motif of 115–130 amino acid residues, referred to as the carbohydrate recognition domain (CRD). The C-type designation is from their requirement for calcium for binding.
Anita Gupta, G. S. Gupta
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C-type lectin receptors in antifungal immunity
Trends in Microbiology, 2008Fungal infections represent a significant health burden, especially in immunocompromised individuals, yet many of the underlying immunological mechanisms involved in the recognition and control of these pathogens are unclear. The identification of the Toll-like receptors (TLRs) has shed new insights on innate microbial recognition and the initiation of
Gordon D. Brown, Janet A. Willment
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Current Opinion in Structural Biology, 1999
Carbohydrate-recognition domains of C-type (Ca2+-dependent) animal lectins serve as prototypes for an important family of protein modules. Only some domains in this family bind Ca2+ or sugars. A comparison of recent structures of C-type lectin-like domains reveals diversity in the modular fold, particularly in the region associated with Ca2+ and sugar ...
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Carbohydrate-recognition domains of C-type (Ca2+-dependent) animal lectins serve as prototypes for an important family of protein modules. Only some domains in this family bind Ca2+ or sugars. A comparison of recent structures of C-type lectin-like domains reveals diversity in the modular fold, particularly in the region associated with Ca2+ and sugar ...
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The C‐type lectin superfamily in the immune system
Immunological Reviews, 1998Summary: Protein‐carbohydrate interactions serve multiple functions in the immune system. Many animal lectins (sugar‐binding proteins) mediate both pathogen recognition and cell‐cell interactions using structurally related Ca2+‐dependent carbohydrate‐recognition domains (C‐type CRDs).
Maureen E. Taylor +2 more
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