3ltg: Difference between revisions

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[[Image:3ltg.png|left|200px]]
==Crystal structure of the Drosophila Epidermal Growth Factor Receptor ectodomain complexed with a low affinity Spitz mutant==
<StructureSection load='3ltg' size='340' side='right' caption='[[3ltg]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3ltg]] is a 3 chain structure with sequence 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LTG FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i2t|3i2t]], [[3ltf|3ltf]], [[3ca7|3ca7]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">torpedo; dEGFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]), Spitz ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ltg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ltg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ltg RCSB], [http://www.ebi.ac.uk/pdbsum/3ltg PDBsum]</span></td></tr>
</table>
== 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/initialview01.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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_3ltg|  PDB=3ltg  |  SCENE=  }}
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>


===Crystal structure of the Drosophila Epidermal Growth Factor Receptor ectodomain complexed with a low affinity Spitz mutant===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_20723758}}
 
==About this Structure==
[[3ltg]] is a 3 chain structure with sequence 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].


==See Also==
==See Also==
*[[Epidermal Growth Factor Receptor|Epidermal Growth Factor Receptor]]
*[[Epidermal Growth Factor Receptor|Epidermal Growth Factor Receptor]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:020723758</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Alvarado, D.]]
[[Category: Alvarado, D]]
[[Category: Klein, D E.]]
[[Category: Klein, D E]]
[[Category: Lemmon, M A.]]
[[Category: Lemmon, M A]]
[[Category: Atp-binding]]
[[Category: Atp-binding]]
[[Category: Cell membrane]]
[[Category: Cell membrane]]

Revision as of 12:47, 9 December 2014

Crystal structure of the Drosophila Epidermal Growth Factor Receptor ectodomain complexed with a low affinity Spitz mutantCrystal structure of the Drosophila Epidermal Growth Factor Receptor ectodomain complexed with a low affinity Spitz mutant

Structural highlights

3ltg is a 3 chain structure with sequence from Drosophila melanogaster. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:torpedo; dEGFR (Drosophila melanogaster), Spitz (Drosophila melanogaster)
Resources:FirstGlance, OCA, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Alvarado D, Klein DE, Lemmon MA. Structural basis for negative cooperativity in growth factor binding to an EGF receptor. Cell. 2010 Aug 20;142(4):568-79. PMID:20723758 doi:10.1016/j.cell.2010.07.015

3ltg, resolution 3.40Å

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