1flt: Difference between revisions

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-[[Image:1flt.png|left|200px]]
-{{STRUCTURE_1flt|  PDB=1flt  |  SCENE=  }}
+==VEGF IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR==
+<StructureSection load='1flt' size='340' side='right'caption='[[1flt]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1flt]] 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=1FLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FLT 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]] 1.7&#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=1flt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1flt OCA], [https://pdbe.org/1flt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1flt RCSB], [https://www.ebi.ac.uk/pdbsum/1flt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1flt ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/VEGFA_HUMAN VEGFA_HUMAN] Defects in VEGFA are a cause of susceptibility to microvascular complications of diabetes type 1 (MVCD1) [MIM:[https://omim.org/entry/603933 603933]. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis.
+== Function ==
+[https://www.uniprot.org/uniprot/VEGFA_HUMAN VEGFA_HUMAN] Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. NRP1/Neuropilin-1 binds isoforms VEGF-165 and VEGF-145. Isoform VEGF165B binds to KDR but does not activate downstream signaling pathways, does not activate angiogenesis and inhibits tumor growth.<ref>PMID:11427521</ref> <ref>PMID:15520188</ref> <ref>PMID:16489009</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/fl/1flt_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=1flt ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Vascular endothelial growth factor (VEGF) is a homodimeric hormone that induces proliferation of endothelial cells through binding to the kinase domain receptor and the Fms-like tyrosine kinase receptor (Flt-1), the extracellular portions of which consist of seven immunoglobulin domains. We show that the second and third domains of Flt-1 are necessary and sufficient for binding VEGF with near-native affinity, and that domain 2 alone binds only 60-fold less tightly than wild-type. The crystal structure of the complex between VEGF and the second domain of Flt-1 shows domain 2 in a predominantly hydrophobic interaction with the "poles" of the VEGF dimer. Based on this structure and on mutational data, we present a model of VEGF bound to the first four domains of Flt-1.
-===VEGF IN COMPLEX WITH DOMAIN 2 OF THE FLT-1 RECEPTOR===
+Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor.,Wiesmann C, Fuh G, Christinger HW, Eigenbrot C, Wells JA, de Vos AM Cell. 1997 Nov 28;91(5):695-704. PMID:9393862<ref>PMID:9393862</ref>
-{{ABSTRACT_PUBMED_9393862}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-==About this Structure==
+<div class="pdbe-citations 1flt" style="background-color:#fffaf0;"></div>
-[[1flt]] is a 4 chain structure with 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=1FLT OCA].
 ==See Also==
-*[[Tyrosine kinase|Tyrosine kinase]]
+*[[VEGF 3D Structures|VEGF 3D Structures]]
-*[[Vascular Endothelial Growth Factor|Vascular Endothelial Growth Factor]]
+== References ==
+<references/>
-==Reference==
+__TOC__
-<ref group="xtra">PMID:009393862</ref><references group="xtra"/>
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Receptor protein-tyrosine kinase]]
+[[Category: Large Structures]]
-[[Category: Vos, A M.De.]]
+[[Category: De Vos AM]]
-[[Category: Wiesmann, C.]]
+[[Category: Wiesmann C]]
-[[Category: Cystine knot]]
-[[Category: Flt-1 receptor]]
-[[Category: Glycoprotein]]
-[[Category: Immunoglobulin-like domain transferase]]