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

ABSTRACT: 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.

SUBMITTER: Mortl M

PROVIDER: S-EPMC2204121 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature

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

Mörtl Mario M Sonderegger Peter P Diederichs Kay K Welte Wolfram W

Protein science : a publication of the Protein Society 20070831 10

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 molec ...[more]

PMID: 17766378

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