3ltg: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:3ltg.png|left|200px]]
-<!--
+==Crystal structure of the Drosophila Epidermal Growth Factor Receptor ectodomain complexed with a low affinity Spitz mutant==
-The line below this paragraph, containing "STRUCTURE_3ltg", creates the "Structure Box" on the page.
+<StructureSection load='3ltg' size='340' side='right'caption='[[3ltg]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3ltg]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LTG FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
--->
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ltg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ltg OCA], [https://pdbe.org/3ltg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ltg RCSB], [https://www.ebi.ac.uk/pdbsum/3ltg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ltg ProSAT]</span></td></tr>
-{{STRUCTURE_3ltg|  PDB=3ltg  |  SCENE=  }}
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/EGFR_DROME EGFR_DROME] Binds to four ligands: Spitz, Gurken, Vein and Argos, which is an antagonist. Transduces the signal through the ras-raf-MAPK pathway. Involved in a myriad of developmental decisions. Critical for the proliferation of imaginal tissues, and for the determination of both the antero-posterior and dorso-ventral polarities of the oocyte. In the embryo, plays a role in the establishment of ventral cell fates, maintenance of amnioserosa and ventral neuroectodermal cells, germ band retraction, cell fate specification in the central nervous system and production of cuticle. Required for embryonic epithelial tissue repair.<ref>PMID:22140578</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lt/3ltg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=3ltg ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Transmembrane signaling by the epidermal growth factor receptor (EGFR) involves ligand-induced dimerization and allosteric regulation of the intracellular tyrosine kinase domain. Crystallographic studies have shown how ligand binding induces dimerization of the EGFR extracellular region but cannot explain the "high-affinity" and "low-affinity" classes of cell-surface EGF-binding sites inferred from curved Scatchard plots. From a series of crystal structures of the Drosophila EGFR extracellular region, we show here how Scatchard plot curvature arises from negatively cooperative ligand binding. The first ligand-binding event induces formation of an asymmetric dimer with only one bound ligand. The unoccupied site in this dimer is structurally restrained, leading to reduced affinity for binding of the second ligand, and thus negative cooperativity. Our results explain the cell-surface binding characteristics of EGF receptors and suggest how individual EGFR ligands might stabilize distinct dimeric species with different signaling properties.
-===Crystal structure of the Drosophila Epidermal Growth Factor Receptor ectodomain complexed with a low affinity Spitz mutant===
+Structural basis for negative cooperativity in growth factor binding to an EGF receptor.,Alvarado D, Klein DE, Lemmon MA Cell. 2010 Aug 20;142(4):568-79. PMID:20723758<ref>PMID:20723758</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3ltg" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_20723758}}, adds the Publication Abstract to the page
+*[[Epidermal growth factor receptor 3D structures|Epidermal growth factor receptor 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 20723758 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20723758}}
+__TOC__
+</StructureSection>
-==About this Structure==
-LTG is a 3 chains structure with sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LTG OCA].
-==Reference==
-<ref group="xtra">PMID:20723758</ref><references group="xtra"/>
 [[Category: Drosophila melanogaster]]
-[[Category: Alvarado, D.]]
+[[Category: Large Structures]]
-[[Category: Klein, D E.]]
+[[Category: Alvarado D]]
-[[Category: Lemmon, M A.]]
+[[Category: Klein DE]]
-[[Category: Atp-binding]]
+[[Category: Lemmon MA]]
-[[Category: Cell membrane]]
-[[Category: Developmental protein]]
-[[Category: Differentiation]]
-[[Category: Disulfide bond]]
-[[Category: Egf-like domain]]
-[[Category: Endoplasmic reticulum]]
-[[Category: Glycoprotein]]
-[[Category: Golgi apparatus]]
-[[Category: Kinase]]
-[[Category: Membrane]]
-[[Category: Neurogenesis]]
-[[Category: Nucleotide-binding]]
-[[Category: Receptor]]
-[[Category: Receptor-ligand complex ectodomain cysteine rich domain egf domain]]
-[[Category: Transferase]]
-[[Category: Transferase-transferase regulator complex]]
-[[Category: Transmembrane]]
-[[Category: Tyrosine-protein kinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Sep 10 13:30:22 2010''