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| {{STRUCTURE_2c5d| PDB=2c5d | SCENE= }} | | {{STRUCTURE_2c5d| PDB=2c5d | SCENE= }} |
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| '''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX'''
| | ===STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_16362042}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16362042 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16362042}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Receptor tyrosine kinase]] | | [[Category: Receptor tyrosine kinase]] |
| [[Category: Vitamin k-dependent protein]] | | [[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 Sun Jul 27 23:13:58 2008'' |
