C-type lectin-like domains

Drickamer, K. (1999). C-type lectin-like domains. Curr. Opin. Struct. Biol. 9(5), 585—590. Farag, S. S., Fehniger, T. A., Ruggeri, L., Velardi, A., and Caligiuri, M. A. (2002). Natural killer cell receptors New biology and insights into the graft-versus-leuke-mia effect. Blood 100(6), 1935-1947. 

Llera, A. S., Viedma, F., Sanchez-Madrid, F., and Tormo, J. (2001). Crystal structure of the C-type lectin-like domain from the human hematopoietic cell receptor CD69. /. Biol. Chem. 276(10), 7312-7319. 

The mannose receptor subfamily is a group of membrane-attached C-type lectins with multiple CRDs. Since most of these domains maintain neither calcium-binding nor sugarbinding properties, the term C-type lectin-like domain (CTLD) is more frequently used lately instead of the term CRD. The mannose receptor subfamily comprises four members including the mannose receptor, the M-type phospholipase A2... 

K. Drickamer, C-type lectin-like domains, Curr. Opin. Struct. Biol. 1999, 9, 585-590. 

C-type lectin receptors (CLRs) are a family of proteins containing one or more structurally-related C-type, lectin-like domains. Transmembrane CLRs which mediate fungal binding include the mannose receptor (MR), Dectin 1, Dectin 2 and the dendritic cell receptor, DC-SIGN (reviewed in). ... 

Takeya, H., Nishida, S., Miyata, T, Kawada, S., Saisaka, Y, Morita, T, and Iwanaga, S., 1992, Coagulation factor X activating enzyme from Russell s viper venom (RVV-X). A novel metalloproteinase with disintegrin (platelet aggregation inhibitor)-like and C-type lectin-like domains, J. Biol Chem. 267 14109-14117. 

Fig. 6.12 Peptide domains and attached glycosaminoglycans in aggrecan and versican. HABR Hyaluronic Acid-Binding Region GAG Glycosaminoglycan-Attachment domain EGF Epidermal Growth Factor-like repeat LEC C-type Lectin-like module C (yellow) Complement regulatory protein-like module (see text) (From GlycoWord website http //www.glycoforum. gr.jp/science/word/proteoglycan/PGA03E.html (contributed by Toshikazu Yada))...

Figure 47-10. Schematic diagram of the structure of human L-selectin. The extracellular portion contains an amino terminal domain homologous to C-type lectins and an adjacent epidermal growth factor-like domain. These are followed by a variable number of complement regulatory-like modules (numbered circles) and a transmembrane sequence (blackdiamond). A short cytoplasmic sequence (open rectangle) is at the carboxyl terminal. The structures of P- and E-selectin are similar to that shown except that they contain more complement-regulatory modules.The numbers of amino acids in L-, P-, and E- selectins, as deduced from the cDNA sequences, are 385,789, and 589, respectively. (Reproduced, with permission, from Bevilacqua MP, Nelson RM Selectins. J Clin Invest 1993 91 370.)...

There are three types of selectins responsible for the attachment of leukocytes to the endothelium, as shown in Table 3.1. Selectins possess three types of domains a C-type lectin domain, an epidermal growth-factor-like domain and between two and nine regulatory domains. 

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