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 |
| + | |PDB= 2c5d |SIZE=350|CAPTION= <scene name='initialview01'>2c5d</scene>, resolution 3.3Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2C5D is a [ | + | 2C5D is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5D OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/16362042 16362042] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: vitamin k-dependent protein]] | [[Category: vitamin k-dependent protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:11:02 2008'' |
Revision as of 14:11, 20 March 2008
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| , resolution 3.3Å | |||||||
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| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Transferred entry: 2.7.10.1 and 2.7.10.2, with EC number 2.7.1.112 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 16:11:02 2008
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
