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1h30

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C-terminal LG domain pair of human Gas6

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Retrieved from "http://52.214.119.220/wiki/index.php/1h30"

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-[[Image:1h30.gif|left|200px]]
- {{Structure
+==C-terminal LG domain pair of human Gas6==
-|PDB= 1h30 |SIZE=350|CAPTION= <scene name='initialview01'>1h30</scene>, resolution 2.2&Aring;
+<StructureSection load='1h30' size='340' side='right'caption='[[1h30]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-|SITE= <scene name='pdbsite=CAA:So4+Binding+Site+For+Chain+A'>CAA</scene>
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1h30]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H30 FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h30 OCA], [https://pdbe.org/1h30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h30 RCSB], [https://www.ebi.ac.uk/pdbsum/1h30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h30 ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h30 OCA], [http://www.ebi.ac.uk/pdbsum/1h30 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h30 RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/GAS6_HUMAN GAS6_HUMAN] Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses.<ref>PMID:12364394</ref> <ref>PMID:18840707</ref>
+== Evolutionary Conservation ==
-'''C-TERMINAL LG DOMAIN PAIR OF HUMAN GAS6'''
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
-==Overview==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/h3/1h30_consurf.spt"</scriptWhenChecked>
-Receptor tyrosine kinases of the Axl family are activated by Gas6, the product of growth arrest-specific gene 6. Gas6-Axl signaling is implicated in cell survival, adhesion, and migration. The receptor-binding site of Gas6 is located within a C-terminal pair of laminin G-like (LG) domains that do not resemble any other receptor tyrosine kinase ligand. We report the crystal structure at 2.2-A resolution of a Gas6 fragment spanning both LG domains (Gas6-LG). The structure reveals a V-shaped arrangement of LG domains strengthened by an interdomain calcium-binding site. LG2 of Gas6-LG contains two unusual features: an alpha-helix cradled by one edge of the LG beta-sandwich and a conspicuous patch of surface-exposed hydrophobic residues. Mutagenesis of some residues in this patch reduces Gas6-LG binding to the extracellular domain of Axl as well as Axl activation in glioblastoma cells, identifying a component of the receptor-binding site of Gas6.
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==About this Structure==
+  </jmolCheckbox>
-H30 is a [[Single protein]] structure of sequence 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=1H30 OCA].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1h30 ConSurf].
+<div style="clear:both"></div>
-==Reference==
+== References ==
-Crystal structure of a C-terminal fragment of growth arrest-specific protein Gas6. Receptor tyrosine kinase activation by laminin G-like domains., Sasaki T, Knyazev PG, Cheburkin Y, Gohring W, Tisi D, Ullrich A, Timpl R, Hohenester E, J Biol Chem. 2002 Nov 15;277(46):44164-70. Epub 2002 Sep 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12218057 12218057]
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Cheburkin, Y.]]
+[[Category: Cheburkin Y]]
-[[Category: Gohring, W.]]
+[[Category: Gohring W]]
-[[Category: Hohenester, E.]]
+[[Category: Hohenester E]]
-[[Category: Knyazev, P G.]]
+[[Category: Knyazev PG]]
-[[Category: Sasaki, T.]]
+[[Category: Sasaki T]]
-[[Category: Timpl, R.]]
+[[Category: Timpl R]]
-[[Category: Tisi, D.]]
+[[Category: Tisi D]]
-[[Category: Ullrich, A.]]
+[[Category: Ullrich A]]
-[[Category: axl/sky/mer ligand]]
-[[Category: calcium-binding]]
-[[Category: egf-like domain]]
-[[Category: laminin g-like domain]]
-[[Category: vitamin k-dependent protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:56:41 2008''

1h30

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Current revision

C-terminal LG domain pair of human Gas6

Structural highlights

Function

Evolutionary Conservation

References

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