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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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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78606

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78238

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons77854

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;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78812

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

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78797

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: http://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.