View source for 3dye


==Crystal structure of AED7-norepineprhine complex==
<StructureSection load='3dye' size='340' side='right'caption='[[3dye]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3dye]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3DYE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DYE 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]] 1.75&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LNR:L-NOREPINEPHRINE'>LNR</scene></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=3dye FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dye OCA], [https://pdbe.org/3dye PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dye RCSB], [https://www.ebi.ac.uk/pdbsum/3dye PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dye ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/D7L1_AEDAE D7L1_AEDAE] Modulates blood feeding of female mosquitoes on vertebrate species by binding and sequestering different mediators involved in the host response, such as biogenic amines and eicosanoids (PubMed:32799410, PubMed:37909749). Binds serotonin, histamine, leukotriene B4, leukotriene C4, leukotriene D4, leukotriene E4, adrenaline and noradrenaline (PubMed:16301315, PubMed:19234127, PubMed:32799410). Does not bind tryptamine and U-46619, a stable analog of thromboxane A2 (PubMed:19234127, PubMed:32799410). Exhibits vasodilating activity (PubMed:32799410). Inhibits agonist-induced platelet aggregation but not blood clotting (PubMed:32799410). Inhibits noradrenaline-induced smooth muscle contraction (PubMed:16301315). Promotes an influx of host neutrophils at the inoculation site (PubMed:38378891).<ref>PMID:16301315</ref> <ref>PMID:19234127</ref> <ref>PMID:32799410</ref> <ref>PMID:37909749</ref> <ref>PMID:38378891</ref>   (Microbial infection) Probably promotes Plasmodium gallinaceum oocyst development in mosquito midgut.<ref>PMID:37909749</ref>   (Microbial infection) Exhibits antiviral activity against dengue virus type 2 probably through a direct interaction with dengue virus virions.<ref>PMID:27632170</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/dy/3dye_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=3dye ConSurf].
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== Publication Abstract from PubMed ==
The mosquito D7 salivary proteins are encoded by a multigene family related to the arthropod odorant-binding protein (OBP) superfamily. Forms having either one or two OBP domains are found in mosquito saliva. Four single-domain and one two-domain D7 proteins from Anopheles gambiae and Aedes aegypti (AeD7), respectively, were shown to bind biogenic amines with high affinity and with a stoichiometry of one ligand per protein molecule. Sequence comparisons indicated that only the C-terminal domain of AeD7 is homologous to the single-domain proteins from A. gambiae, suggesting that the N-terminal domain may bind a different class of ligands. Here, we describe the 3D structure of AeD7 and examine the ligand-binding characteristics of the N- and C-terminal domains. Isothermal titration calorimetry and ligand complex crystal structures show that the N-terminal domain binds cysteinyl leukotrienes (cysLTs) with high affinities (50-60 nM) whereas the C-terminal domain binds biogenic amines. The lipid chain of the cysLT binds in a hydrophobic pocket of the N-terminal domain, whereas binding of norepinephrine leads to an ordering of the C-terminal portion of the C-terminal domain into an alpha-helix that, along with rotations of Arg-176 and Glu-268 side chains, acts to bury the bound ligand.

Multifunctionality and mechanism of ligand binding in a mosquito antiinflammatory protein.,Calvo E, Mans BJ, Ribeiro JM, Andersen JF Proc Natl Acad Sci U S A. 2009 Mar 10;106(10):3728-33. Epub 2009 Feb 20. PMID:19234127<ref>PMID:19234127</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Aedes aegypti]]
[[Category: Large Structures]]
[[Category: Andersen JF]]
[[Category: Calvo E]]
[[Category: Mans BJ]]
[[Category: Ribeiro JM]]