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          Institute: MPI für Biochemie     Collection: Molecular Medicine (R. Fässler)     Display Documents



ID: 41715.0, MPI für Biochemie / Molecular Medicine (R. Fässler)
Crystal structure of a C-terminal fragment of growth arrest- specific protein Gas6 - Receptor tyrosine kinase activation by laminin G-like domains
Authors:Sasaki, T.; Knyazev, P. G.; Cheburkin, Y.; Göhring, W.; Tisi, D.; Ullrich, A.; Timpl, R.; Hohenester, E.
Language:English
Date of Publication (YYYY-MM-DD):2002-11-15
Title of Journal:Journal of Biological Chemistry
Journal Abbrev.:J. Biol. Chem.
Volume:277
Issue / Number:46
Start Page:44164
End Page:44170
Review Status:Peer-review
Audience:Not Specified
Abstract / Description: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.
Comment of the Author/Creator:Date: 2002, NOV 15
External Publication Status:published
Document Type:Article
Communicated by:N.N.
Affiliations:MPI für Biochemie/Molecular Medicine (R. Fässler)/Extracellular Matrix Proteins (T. Sasaki)
MPI für Biochemie/Molecular Biology (A. Ullrich)
MPI für Biochemie/Emeriti Groups/Protein Chemistry (R. Timpl)
External Affiliations:Univ London Imperial Coll Sci Technol & Med, Blackett Lab,; Biophys Sect, Dept Biol Sci, Prince Consort Rd, London SW7 2BW,; England; Univ London Imperial Coll Sci Technol & Med, Blackett Lab, Biophys Sect, Dept Biol Sci, London SW7 2BW, England
Identifiers:ISI:000179272000082 [ID No:1]
ISSN:0021-9258 [ID No:2]
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