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J. Biol. Chem., Vol. 281, Issue 47, 36052-36059, November 24, 2006

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A Novel -Helix in the First Fibronectin Type III Repeat of the Neural Cell Adhesion Molecule Is Critical for N-Glycan Polysialylation^*

Shalu Shiv Mendiratta, Nikolina Sekulic, Francisco G. Hernandez-Guzman, Brett E. Close, Arnon Lavie, and Karen J. Colley¹

From the Department of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60607 and Accelrys, Inc., San Diego, California 92121

Polysialic acid is a developmentally regulated, anti-adhesive glycan that is added to the neural cell adhesion molecule, NCAM. Polysialylated NCAM is critical for brain development and plays roles in synaptic plasticity, axon guidance, and cell migration. The first fibronectin type III repeat of NCAM, FN1, is necessary for the polysialylation of N-glycans on the adjacent immunoglobulin domain. This repeat cannot be replaced by other fibronectin type III repeats. We solved the crystal structure of human NCAM FN1 and found that, in addition to a unique acidic surface patch, it possesses a novel -helix that links strands 4 and 5 of its -sandwich structure. Replacement of the -helix did not eliminate polysialyltransferase recognition, but shifted the addition of polysialic acid from the N-glycans modifying the adjacent immunoglobulin domain to O-glycans modifying FN1. Other experiments demonstrated that replacement of residues in the acidic surface patch alter the polysialylation of both N- and O-glycans in the same way, while the -helix is only required for the polysialylation of N-glycans. Our data are consistent with a model in which the FN1 -helix is involved in an Ig5-FN1 interaction that is critical for the correct positioning of Ig5 N-glycans for polysialylation.

Received for publication, August 22, 2006 , and in revised form, September 22, 2006.

The atomic coordinates and structure factors (code 2HAZ) 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 National Institutes of Health Grant R01GM63843 (to K. J. C.). 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 Biochemistry and Molecular Genetics, University of Illinois at Chicago, College of Medicine, 900 S. Ashland Ave. M/C 669, Chicago, IL 60607. Tel.: 312-996-7756; Fax: 312-413-0353; E-mail: karenc{at}uic.edu.

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