1H30

C-terminal LG domain pair of human Gas6

Summary for 1H30

• Entry DOI: 10.2210/pdb1h30/pdb
• Descriptor: GROWTH-ARREST-SPECIFIC PROTEIN, CALCIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: laminin g-domain protein, vitamin k-dependent protein, axl/sky/mer ligand, laminin g- like domain, egf-like domain, calcium-binding
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Secreted: Q14393
• Total number of polymer chains: 1
• Total formula weight: 46847.56

Authors

Sasaki, T.,Knyazev, P.G.,Cheburkin, Y.,Gohring, W.,Tisi, D.,Ullrich, A.,Timpl, R.,Hohenester, E. (deposition date: 2002-08-21, release date: 2003-01-30, Last modification date: 2024-11-13)

Primary citation

Sasaki, T.,Knyazev, P.G.,Cheburkin, Y.,Gohring, W.,Tisi, D.,Ullrich, A.,Timpl, R.,Hohenester, E.
Crystal Structure of a Carboxy-Terminal Fragment of Growth-Arrest-Specific Protein Gas6: Receptor Tyrosine Kinase Activation by Laminin G-Like Domains
J.Biol.Chem., 277:44164-, 2002

PubMed 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-A 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 alpha-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.

PubMed: 12218057
DOI: 10.1074/JBC.M207340200

Experimental method

X-RAY DIFFRACTION (2.2 Å)