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

Mörtl, Mario; Sonderegger, Peter; Diederichs, Kay; Welte, Wolfram

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

Dateien

Mörtl_etal_Crystal.pdfGröße: 5.56 MBDownloads: 1031

Datum

2007

Autor:innen

Mörtl, Mario

Sonderegger, Peter

Diederichs, Kay

Welte, Wolfram

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Chemie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Protein Science. 2007, 16(10), pp. 2174-2183. ISSN 0961-8368. eISSN 1469-896X. Available under: doi: 10.1110/ps.072802707

Zusammenfassung

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.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

Protein structure, cell adhesion, TAG-1, buried surface

Zitieren

ISO 690

MÖRTL, Mario, Peter SONDEREGGER, Kay DIEDERICHS, Wolfram WELTE, 2007. The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction. In: Protein Science. 2007, 16(10), pp. 2174-2183. ISSN 0961-8368. eISSN 1469-896X. Available under: doi: 10.1110/ps.072802707

BibTex

@article{Mortl2007-10cryst-20862,
  year={2007},
  doi={10.1110/ps.072802707},
  title={The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction},
  number={10},
  volume={16},
  issn={0961-8368},
  journal={Protein Science},
  pages={2174--2183},
  author={Mörtl, Mario and Sonderegger, Peter and Diederichs, Kay and Welte, Wolfram}
}

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Universitätsbibliographie

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