Publikation: The crystal structure of the ligand-binding module of human TAG-1 suggests a new mode of homophilic interaction
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2007
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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.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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Protein structure, cell adhesion, TAG-1, buried surface
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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.072802707BibTex
@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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