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The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction

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-1_Ig1–4), 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

Abbreviations: IgSF, immunoglobulin superfamily; Ig domain, immunoglobulin-like domain; FnIII domain, fibronectin III-like domain; CV, column volume(s); B, buried surface; f _np B, nonpolar interface area; f _bu, fraction of fully buried atoms; RP, residue propensity score; S _C, shape complementarity value; R _work or R _free, R factor (defined in Table 2).

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.072802707.

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