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2c5d

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[[Image:2c5d.gif|left|200px]]<br /><applet load="2c5d" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2c5d.gif|left|200px]]
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caption="2c5d, resolution 3.3&Aring;" />
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'''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX'''<br />
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{{Structure
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|PDB= 2c5d |SIZE=350|CAPTION= <scene name='initialview01'>2c5d</scene>, resolution 3.3&Aring;
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|SITE= <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene>
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|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>
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|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]
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|GENE=
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}}
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'''STRUCTURE OF A MINIMAL GAS6-AXL COMPLEX'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=NI:'>NI</scene> and <scene name='pdbligand=SO4:'>SO4</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=2C5D OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=16362042 16362042]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:45:05 2008''
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''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


PDB ID 2c5d

Drag the structure with the mouse to rotate
, resolution 3.3Å
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

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