2c5d: Difference between revisions

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==Overview==
==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 ... [[http://ispc.weizmann.ac.il/pmbin/getpm?16362042 (full description)]]
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==
==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]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C5D OCA]].  
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] Structure known Active Site: AC1. 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]]


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