2c5d
From Proteopedia
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[[Image:2c5d.gif|left|200px]] | [[Image:2c5d.gif|left|200px]] | ||
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'''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX''' | '''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX''' | ||
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[[Category: Timpl, R.]] | [[Category: Timpl, R.]] | ||
[[Category: Ullrich, A.]] | [[Category: Ullrich, A.]] | ||
- | [[Category: | + | [[Category: Egf-like domain]] |
- | [[Category: | + | [[Category: Growth regulation]] |
- | [[Category: | + | [[Category: Immunoglobulin-like domain]] |
- | [[Category: | + | [[Category: Laminin g-like domain]] |
- | [[Category: | + | [[Category: Receptor]] |
- | [[Category: | + | [[Category: Receptor tyrosine kinase]] |
- | [[Category: | + | [[Category: Vitamin k-dependent protein]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:16:38 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 18:16, 3 May 2008
STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX
Overview
Receptor tyrosine kinases of the Axl family are activated by the vitamin K-dependent protein Gas6. Axl signalling plays important roles in cancer, spermatogenesis, immunity, and platelet function. The crystal structure at 3.3 A resolution of a minimal human Gas6/Axl complex reveals an assembly of 2:2 stoichiometry, in which the two immunoglobulin-like domains of the Axl ectodomain are crosslinked by the first laminin G-like domain of Gas6, with no direct Axl/Axl or Gas6/Gas6 contacts. There are two distinct Gas6/Axl contacts of very different size, both featuring interactions between edge beta-strands. Structure-based mutagenesis, protein binding assays and receptor activation experiments demonstrate that both the major and minor Gas6 binding sites are required for productive transmembrane signalling. Gas6-mediated Axl dimerisation is likely to occur in two steps, with a high-affinity 1:1 Gas6/Axl complex forming first. Only the minor Gas6 binding site is highly conserved in the other Axl family receptors, Sky/Tyro3 and Mer. Specificity at the major contact is suggested to result from the segregation of charged and apolar residues to opposite faces of the newly formed beta-sheet.
About this Structure
2C5D is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural basis for Gas6-Axl signalling., Sasaki T, Knyazev PG, Clout NJ, Cheburkin Y, Gohring W, Ullrich A, Timpl R, Hohenester E, EMBO J. 2006 Jan 11;25(1):80-7. Epub 2005 Dec 15. PMID:16362042 Page seeded by OCA on Sat May 3 21:16:38 2008
Categories: Homo sapiens | Protein complex | Transferase | Cheburkin, Y. | Clout, N J. | Goehring, W. | Hohenester, E. | Knyazev, P G. | Sasaki, T. | Timpl, R. | Ullrich, A. | Egf-like domain | Growth regulation | Immunoglobulin-like domain | Laminin g-like domain | Receptor | Receptor tyrosine kinase | Vitamin k-dependent protein