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2xac

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==Structural Insights into the Binding of VEGF-B by VEGFR-1D2: Recognition and Specificity==
==Structural Insights into the Binding of VEGF-B by VEGFR-1D2: Recognition and Specificity==
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<StructureSection load='2xac' size='340' side='right' caption='[[2xac]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
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<StructureSection load='2xac' size='340' side='right'caption='[[2xac]], [[Resolution|resolution]] 2.71&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2xac]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XAC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XAC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2xac]] is a 4 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=2XAC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XAC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.71&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1rv6|1rv6]], [[2c7w|2c7w]], [[1qsv|1qsv]], [[2vwe|2vwe]], [[1qty|1qty]], [[1qsz|1qsz]], [[1flt|1flt]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Receptor_protein-tyrosine_kinase Receptor protein-tyrosine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 2.7.10.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xac OCA], [https://pdbe.org/2xac PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xac RCSB], [https://www.ebi.ac.uk/pdbsum/2xac PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xac ProSAT]</span></td></tr>
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<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=2xac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xac OCA], [http://pdbe.org/2xac PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xac RCSB], [http://www.ebi.ac.uk/pdbsum/2xac PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xac ProSAT]</span></td></tr>
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</table>
</table>
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== Disease ==
 
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[[http://www.uniprot.org/uniprot/VGFR1_HUMAN VGFR1_HUMAN]] Note=Can contribute to cancer cell survival, proliferation, migration, and invasion, and tumor angiogenesis and metastasis. May contribute to cancer pathogenesis by promoting inflammatory responses and recruitment of tumor-infiltrating macrophages. Note=Abnormally high expression of soluble isoforms (isoform 2, isoform 3 or isoform 4) may be a cause of preeclampsia.
 
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VEGFB_HUMAN VEGFB_HUMAN]] Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis. [[http://www.uniprot.org/uniprot/VGFR1_HUMAN VGFR1_HUMAN]] Tyrosine-protein kinase that acts as a cell-surface receptor for VEGFA, VEGFB and PGF, and plays an essential role in the development of embryonic vasculature, the regulation of angiogenesis, cell survival, cell migration, macrophage function, chemotaxis, and cancer cell invasion. May play an essential role as a negative regulator of embryonic angiogenesis by inhibiting excessive proliferation of endothelial cells. Can promote endothelial cell proliferation, survival and angiogenesis in adulthood. Its function in promoting cell proliferation seems to be cell-type specific. Promotes PGF-mediated proliferation of endothelial cells, proliferation of some types of cancer cells, but does not promote proliferation of normal fibroblasts (in vitro). Has very high affinity for VEGFA and relatively low protein kinase activity; may function as a negative regulator of VEGFA signaling by limiting the amount of free VEGFA and preventing its binding to KDR. Likewise, isoforms lacking a transmembrane domain, such as isoform 2, isoform 3 and isoform 4, may function as decoy receptors for VEGFA. Modulates KDR signaling by forming heterodimers with KDR. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate and the activation of protein kinase C. Mediates phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, leading to activation of phosphatidylinositol kinase and the downstream signaling pathway. Mediates activation of MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Phosphorylates SRC and YES1, and may also phosphorylate CBL. Isoform 1 phosphorylates PLCG. Promotes phosphorylation of AKT1 at 'Ser-473'. Promotes phosphorylation of PTK2/FAK1. Isoform 7 has a truncated kinase domain; it increases phosphorylation of SRC at 'Tyr-418' by unknown means and promotes tumor cell invasion.<ref>PMID:8248162</ref> <ref>PMID:18593464</ref> <ref>PMID:18515749</ref> <ref>PMID:20512933</ref> <ref>PMID:7824266</ref> <ref>PMID:8605350</ref> <ref>PMID:9299537</ref> <ref>PMID:11141500</ref> <ref>PMID:11811792</ref> <ref>PMID:11312102</ref> <ref>PMID:14633857</ref> <ref>PMID:12796773</ref> <ref>PMID:15735759</ref> <ref>PMID:16685275</ref> <ref>PMID:18079407</ref> <ref>PMID:18583712</ref> <ref>PMID:20551949</ref> <ref>PMID:21752276</ref>
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[https://www.uniprot.org/uniprot/VEGFB_HUMAN VEGFB_HUMAN] Growth factor for endothelial cells. VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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==See Also==
==See Also==
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*[[Vascular Endothelial Growth Factor|Vascular Endothelial Growth Factor]]
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*[[VEGF 3D Structures|VEGF 3D Structures]]
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*[[Vascular Endothelial Growth Factor Receptor|Vascular Endothelial Growth Factor Receptor]]
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*[[3D structures of vascular endothelial growth factor receptor|3D structures of vascular endothelial growth factor receptor]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Receptor protein-tyrosine kinase]]
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[[Category: Large Structures]]
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[[Category: Acharya, K R]]
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[[Category: Acharya KR]]
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[[Category: Darley, P]]
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[[Category: Darley P]]
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[[Category: Iyer, S]]
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[[Category: Iyer S]]
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[[Category: Angiogenesis]]
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[[Category: Cysteine-knot protein]]
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[[Category: Mitogen]]
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[[Category: Signaling protein]]
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[[Category: Transferase]]
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[[Category: Transferase-signaling protein complex]]
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Current revision

Structural Insights into the Binding of VEGF-B by VEGFR-1D2: Recognition and Specificity

PDB ID 2xac

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