3v6b: Difference between revisions
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The | ==VEGFR-2/VEGF-E complex structure== | ||
<StructureSection load='3v6b' size='340' side='right'caption='[[3v6b]], [[Resolution|resolution]] 3.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3v6b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Orf_virus Orf virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V6B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V6B FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.205Å</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=3v6b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v6b OCA], [https://pdbe.org/3v6b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v6b RCSB], [https://www.ebi.ac.uk/pdbsum/3v6b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v6b ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VEGFH_ORFN2 VEGFH_ORFN2] Induces endothelial proliferation. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Vascular Endothelial Growth Factors (VEGFs) activate three receptor tyrosine kinases, VEGFR-1-3, promoting angiogenic and lymphangiogenic signaling. The extracellular receptor domain (ECD) consists of seven immunoglobulin-homology domains; domains 2 and 3 (D23) represent the ligand binding domain, while the function of D4-7 is unclear. Ligand binding promotes receptor dimerization and instigates transmembrane signaling and receptor kinase activation. Isothermal titration calorimetry showed that the Gibbs free energy of VEGF-A, -C or -E binding to D23 or the full length ECD is dominated by favorable entropic contribution with enthalpic penalty. The free energy of VEGF binding to the ECD is 1.0-1.7 kcal/mol less favorable than for binding to D23. A model of the VEGF-E/VEGFR-2 ECD complex derived from small angle scattering data provided evidence for homotypic interactions in D4-7. We also solved the crystal structures of complexes between VEGF-A or -E with D23 which revealed comparable binding surfaces and similar interactions between the ligands and the receptor, but showed variation in D23 twist angles. The energetically unfavorable homotypic interactions in D4-7 may be required for re-orientation of receptor monomers. This mechanism might prevent ligand-independent activation of VEGFR-2 to evade the deleterious consequences for blood and lymph vessel homeostasis arising from inappropriate receptor activation. | |||
Thermodynamic and structural description of allosterically regulated VEGF receptor 2 dimerization.,Brozzo MS, Bjelic S, Kisko K, Schleier T, Leppanen VM, Alitalo K, Winkler FK, Ballmer-Hofer K Blood. 2011 Dec 29. PMID:22207738<ref>PMID:22207738</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3v6b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[VEGF 3D Structures|VEGF 3D Structures]] | |||
*[[3D structures of vascular endothelial growth factor receptor|3D structures of vascular endothelial growth factor receptor]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Orf virus]] | |||
[[Category: Ballmer-Hofer K]] | |||
[[Category: Brozzo MS]] | |||
[[Category: Kisko K]] | |||
[[Category: Leppanen V-M]] | |||
[[Category: Winkler FK]] | |||
