I-type lectins (siglecs) - sequence alignments
- Siglecs 1, 2 and 4 - CD33-related siglecs
- Introduction to I-type lectins (siglecs)
- Domain organization in siglecs
- Interpro entry: Immunoglobulin
Sequence alignments of human and mouse siglecs 1, 2 and 4
Siglecs 1, 2 and 4 (also known as sialoadhesin/CD169, CD22 and MAG, respectively) are conserved in mammals. Indicated above the alignment are structural domains and potential N-glycosylation sites (+). Cysteine residues are highlighted in yellow. Three residues involved in sialic acid binding are highlighted in magenta and are shown in the structure of siglec-7: the conserved arginine which makes an electrostatic interaction with sialic acid that is essential for high-affinity binding, plus two hydrophobic aromatic residues. Cytoplasmic tyrosine-based signalling motifs are highlighted in orange.
Jump to: Siglec 1 Siglec 2 Siglec 4
If alignments appear scrambled please maximize the width of your browser window.
Structure of Siglec-7 CRD
Structure adapted from Alphey et al, J Biol Chem 278, 3372
