Scavenger Receptor C-Type Lectin Binds to the Leukocyte Cell Surface Glycan Lewis By a Novel Mechanism

Journal Article · Tue Jul 10 04:00:00 EDT 2007 · J.Biol.Chem.282:17250,2007

DOI:https://doi.org/10.1074/jbc.M701624200· OSTI ID:909795

Feinberg, H; Taylor, M E; Weis, W I

The scavenger receptor C-type lectin (SRCL) is unique in the family of class A scavenger receptors, because in addition to binding sites for oxidized lipoproteins it also contains a C-type carbohydrate-recognition domain (CRD) that interacts with specific glycans. Both human and mouse SRCL are highly specific for the Lewis(x) trisaccharide, which is commonly found on the surfaces of leukocytes and some tumor cells. Structural analysis of the CRD of mouse SRCL in complex with Lewis(x) and mutagenesis show the basis for this specificity. The interaction between mouse SRCL and Lewis(x) is analogous to the way that selectins and DC-SIGN bind to related fucosylated glycans, but the mechanism of the interaction is novel, because it is based on a primary galactose-binding site similar to the binding site in the asialoglycoprotein receptor. Crystals of the human receptor lacking bound calcium ions reveal an alternative conformation in which a glycan ligand would be released during receptor-mediated endocytosis.

• Research Organization: Stanford Linear Accelerator Center (SLAC)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC02-76SF00515
• OSTI ID: 909795
• Report Number(s): SLAC-REPRINT-2007-100
• Journal Information: J.Biol.Chem.282:17250,2007, Journal Name: J.Biol.Chem.282:17250,2007 Vol. 282; ISSN 0021-9258; ISSN JBCHA3
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
74 ATOMIC AND MOLECULAR PHYSICS
CALCIUM IONS
LECTINS
LEUKOCYTES
LIPOPROTEINS
MUTAGENESIS
Other
OTHER
SPECIFICITY
TUMOR CELLS