1h30
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 . | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1H30 is a | + | 1H30 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: CAA. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1H30 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vitamin k-dependent protein]] | [[Category: vitamin k-dependent protein]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:01:35 2007'' |
Revision as of 11:56, 5 November 2007
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C-TERMINAL LG DOMAIN PAIR OF HUMAN GAS6
Overview
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.
About this Structure
1H30 is a Single protein structure of sequence from Homo sapiens with CA and SO4 as ligands. Structure known Active Site: CAA. Full crystallographic information is available from OCA.
Reference
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 PG, Cheburkin Y, Gohring W, Tisi D, Ullrich A, Timpl R, Hohenester E, J Biol Chem. 2002 Nov 15;277(46):44164-70. Epub 2002 Sep 5. PMID:12218057
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