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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

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.

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Genre: Journal Article
Alternative Title : J. Biol. Chem.

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 Creators:
Sasaki, T.1, Author              
Knyazev, P. G.2, Author              
Cheburkin, Y.1, 2, Author              
Göhring, W.3, Author
Tisi, D., Author
Ullrich, A.2, Author              
Timpl, R.1, Author              
Hohenester, E., Author
Affiliations:
1Former Research Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565145              
2Ullrich, Axel / Molecular Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565172              
3External Organizations, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2002-11-15
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 41715
ISI: 000179272000082
 Degree: -

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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
 Creator(s):
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Pages: - Volume / Issue: 277 (46) Sequence Number: - Start / End Page: 44164 - 44170 Identifier: ISSN: 0021-9258