Publikation: The Crystal Structure of the Ligand Binding Module of Axonin-1/TAG-1 Suggests a Zipper Mechanism for Neural Cell Adhesion
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We have determined the crystal structure of the ligand binding fragment of the neural cell adhesion molecule axonin-1/TAG-1 comprising the first four immunoglobulin (Ig) domains. The overall structure of axonin-1Ig1 4 is U-shaped due to contacts between domains 1 and 4 and domains 2 and 3. In the crystals, these molecules are aligned in a string with adjacent molecules oriented in an anti-parallel fashion and their C termini perpendicular to the string. This arrangement suggests that cell adhesion by homophilic axonin-1 interaction occurs by the formation of a linear zipper-like array in which the axonin-1 molecules are alternately provided by the two apposed membranes. In accordance with this model, mutations in a loop critical for the formation of the zipper resulted in the loss of the homophilic binding capacity of axonin-1.
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FREIGANG, Jörg, Karl PROBA, Lukas LEDER, Kay DIEDERICHS, Peter SONDEREGGER, Wolfram WELTE, 2000. The Crystal Structure of the Ligand Binding Module of Axonin-1/TAG-1 Suggests a Zipper Mechanism for Neural Cell Adhesion. In: Cell. 2000, 101(4), pp. 425-433. ISSN 0092-8674. Available under: doi: 10.1016/S0092-8674(00)80852-1BibTex
@article{Freigang2000Cryst-7934, year={2000}, doi={10.1016/S0092-8674(00)80852-1}, title={The Crystal Structure of the Ligand Binding Module of Axonin-1/TAG-1 Suggests a Zipper Mechanism for Neural Cell Adhesion}, number={4}, volume={101}, issn={0092-8674}, journal={Cell}, pages={425--433}, author={Freigang, Jörg and Proba, Karl and Leder, Lukas and Diederichs, Kay and Sonderegger, Peter and Welte, Wolfram} }
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