Disease relevance of CLEC1B

• The C-type lectin-like domain (CTLD) of CLEC-2 was expressed in Escherichia coli, refolded and purified [1].

High impact information on CLEC1B

• Tyrosine phosphorylation of CLEC-2 and other signaling proteins by rhodocytin is inhibited by the Src family kinase inhibitor PP2 [2].
• CLEC-2 has a single tyrosine residue in a YXXL motif in its cytosolic tail, which undergoes tyrosine phosphorylation upon platelet activation by rhodocytin or an antibody to CLEC-2, but not to collagen, thrombin receptor agonist peptide (TRAP), or convulxin [2].
• Using rhodocytin affinity chromatography, we have identified a novel C-type lectin receptor, CLEC-2, in platelets that confers signaling responses to rhodocytin when expressed in a cell line [2].
• We have identified two human C-type lectin-like receptors, CLEC-1 and CLEC-2 [3].
• The present study compares the role of PECAM-1 on platelet activation by these two receptors and by the lectin receptor, CLEC-2, which also signals via PLCgamma2 [4].

Biological context of CLEC1B

• CLEC-1 and CLEC-2 genes map to human chromosome 12, most likely in linkage with the NK gene complex (NKC) [3].

Anatomical context of CLEC1B

• CLEC-1 and CLEC-2 are preferentially transcribed in dendritic cells (DC) and in the liver, respectively [3].

Associations of CLEC1B with chemical compounds

• Crystals of this recombinant CLEC-2 were grown by sitting-drop vapour diffusion using polyethylene glycol (PEG) 6000 as a precipitant [1].

Analytical, diagnostic and therapeutic context of CLEC1B

• Crystallization and X-ray diffraction analysis of human CLEC-2 [1].

References