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Published online before print August 31, 2007, 10.1110/ps.072802707
Protein Science (2007), 16:2174-2183. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction

Mario Mörtl1, Peter Sonderegger2, Kay Diederichs1, and Wolfram Welte1

1 University of Konstanz, Department of Biology, D-78464 Konstanz, Germany
2 University of Zürich, Department of Biochemistry, CH-8057 Zürich, Switzerland

(RECEIVED May 4, 2007; FINAL REVISION July 10, 2007; ACCEPTED July 10, 2007)

Human TAG-1 is a neural cell adhesion molecule that is crucial for the development of the nervous system during embryogenesis. It consists of six immunoglobulin-like and four fibronectin III-like domains and is anchored to the membrane by glycosylphosphatidylinositol. Herein we present the crystal structure of the four N-terminal immunoglobulin-like domains of TAG-1 (TAG-1Ig1–4), known to be important in heterophilic and homophilic macromolecular interactions. The contacts of neighboring molecules within the crystal were investigated. A comparison with the structure of the chicken ortholog resulted in an alternative mode for the molecular mechanism of homophilic TAG-1 interaction. This mode of TAG-1 homophilic interaction is based on dimer formation rather than formation of a molecular zipper as proposed for the chicken ortholog.

Keywords: protein structure; cell adhesion; TAG-1; buried surface


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R. M. Gouveia, C. M. Gomes, M. Sousa, P. M. Alves, and J. Costa
Kinetic Analysis of L1 Homophilic Interaction: ROLE OF THE FIRST FOUR IMMUNOGLOBULIN DOMAINS AND IMPLICATIONS ON BINDING MECHANISM
J. Biol. Chem., October 17, 2008; 283(42): 28038 - 28047.
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