2ox9
From Proteopedia
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Mouse Scavenger Receptor C-type Lectin carbohydrate-recognition domain.
Overview
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.
About this Structure
2OX9 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.
Reference
Scavenger receptor C-type lectin binds to the leukocyte cell surface glycan Lewis(x) by a novel mechanism., Feinberg H, Taylor ME, Weis WI, J Biol Chem. 2007 Jun 8;282(23):17250-8. Epub 2007 Apr 9. PMID:17420244
Page seeded by OCA on Wed Jan 23 14:43:43 2008
