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J. Biol. Chem., Vol. 282, Issue 23, 17250-17258, June 8, 2007

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Scavenger Receptor C-type Lectin Binds to the Leukocyte Cell Surface Glycan Lewis^x by a Novel Mechanism^*

Hadar Feinberg, Maureen E. Taylor, and William I. Weis¹

From the Departments of Structural Biology and of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, California 94306 and the Division of Molecular Biosciences, Imperial College, London SW7 2AZ, United Kingdom

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.

Received for publication, February 23, 2007 , and in revised form, March 28, 2007.

The atomic coordinates and structure factors (code 2OX9 and 2OX8) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* This work was supported by Grant GM50565 from the National Institutes of Health (to W. I. W.), Grant 075565 from the Wellcome Trust (to M. E. T.), and Grant GM62116 from the National Institutes of Health to the Consortium for Functional Glycomics. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Structural Biology, Stanford University School of Medicine, 299 Campus Dr. West Stanford, CA 94305-5126. Tel.: 650-725-4623; Fax: 650-723-8464; E-mail: bill.weis{at}stanford.edu.

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