Crystal structure of a C-terminal fragment of growth arrest- specific protein 
Gas6 - Receptor tyrosine kinase activation by laminin G-like domains

Sasaki, T.; Knyazev, P. G.; Cheburkin, Y.; Göhring, W.; Tisi, D.; Ullrich, A.; Timpl, R.; Hohenester, E.

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Crystal structure of a C-terminal fragment of growth arrest- specific protein Gas6 - Receptor tyrosine kinase activation by laminin G-like domains

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Sasaki, T.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Knyazev, P. G.
Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Cheburkin, Y.
Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society;
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Ullrich, A.
Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Timpl, R.
Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society;

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Citation

Sasaki, T., Knyazev, P. G., Cheburkin, Y., Göhring, W., Tisi, D., Ullrich, A., et al. (2002). Crystal structure of a C-terminal fragment of growth arrest- specific protein Gas6 - Receptor tyrosine kinase activation by laminin G-like domains. Journal of Biological Chemistry, 277(46), 44164-44170.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-6DE0-F

Abstract

Receptor tyrosine kinases of the Axl family are activated by Gas6, the product of growth arrest-specific gene 6. Gas6-Axl signaling is implicated in cell survival, adhesion, and migration. The receptor-binding site of Gas6 is located within a C-terminal pair of laminin G-like (LG) domains that do not resemble any other receptor tyrosine kinase ligand. We report the crystal structure at 2.2-Angstrom resolution of a Gas6 fragment spanning both LG domains (Gas6-LG). The structure reveals a V-shaped arrangement of LG domains strengthened by an interdomain calcium-binding site. LG2 of Gas6-LG contains two unusual features: an a-helix cradled by one edge of the LG beta-sandwich and a conspicuous patch of surface-exposed hydrophobic residues. Mutagenesis of some residues in this patch reduces Gas6-LG binding to the extracellular domain of Axl as well as Axl activation in glioblastoma cells, identifying a component of the receptor-binding site of Gas6.