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2c5d
From Proteopedia
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| - | [[Image:2c5d.gif|left|200px]]<br /> | + | [[Image:2c5d.gif|left|200px]]<br /><applet load="2c5d" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2c5d" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2c5d, resolution 3.3Å" /> | caption="2c5d, resolution 3.3Å" /> | ||
'''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX'''<br /> | '''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2C5D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, NI and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.10.1_and_2.7.10.2 Transferred entry: 2.7.10.1 and 2.7.10.2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.112 2.7.1.112] | + | 2C5D is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, NI and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferred_entry:_2.7.10.1_and_2.7.10.2 Transferred entry: 2.7.10.1 and 2.7.10.2], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.112 2.7.1.112] Known structural/functional Site: <scene name='pdbsite=AC1:Nag Binding Site For Chain B'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C5D 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 Tue Dec 18 19:10:33 2007'' |
Revision as of 17:00, 18 December 2007
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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 with CA, NI and SO4 as ligands. Active as Transferred entry: 2.7.10.1 and 2.7.10.2, with EC number 2.7.1.112 Known structural/functional Site: . 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 Tue Dec 18 19:10:33 2007
Categories: Homo sapiens | Protein complex | Transferred entry: 2.7.10.1 and 2.7.10.2 | Cheburkin, Y. | Clout, N.J. | Goehring, W. | Hohenester, E. | Knyazev, P.G. | Sasaki, T. | Timpl, R. | Ullrich, A. | CA | NI | SO4 | Egf-like domain | Growth regulation | Immunoglobulin-like domain | Laminin g-like domain | Receptor | Receptor tyrosine kinase | Vitamin k-dependent protein
