Access
To read this article in full you may need to log in, make a payment or gain access through a site license (see right).
Letter
Nature Chemical Biology 1, 93–97 (1 July 2005) | doi:10.1038/nchembio713
Homomultimeric complexes of CD22 in B cells revealed by protein-glycan cross-linking
&
Abstract
CD22 is a negative regulator of B-cell receptor signaling, an activity mediated by recruitment of SH2 domain–containing phosphatase 1 through a phosphorylated immunoreceptor tyrosine inhibitory motif in its cytoplasmic domain. As in other members of the sialic acid–binding immunoglobulin-like lectin, or siglec, family, the extracellular N-terminal immunoglobulin domain of CD22 binds to glycan ligands containing sialic acid, which are highly expressed on B-cell glycoproteins.
To read this article in full you may need to log in, make a payment or gain access through a site license (see right).
