View source for 4ge1


==Structure of the tryptamine complex of the amine binding protein of Rhodnius prolixus==
<StructureSection load='4ge1' size='340' side='right'caption='[[4ge1]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ge1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodnius_prolixus Rhodnius prolixus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GE1 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]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TSS:2-(1H-INDOL-3-YL)ETHANAMINE'>TSS</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=4ge1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ge1 OCA], [https://pdbe.org/4ge1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ge1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ge1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ge1 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q86PT9_RHOPR Q86PT9_RHOPR] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins that bind small-molecule mediators of inflammation and hemostasis are essential for blood-feeding by arthropod vectors of infectious disease. In ticks and triatomine insects, the lipocalin protein family is greatly expanded and members have been shown to bind biogenic amines, eicosanoids and ADP. These compounds are potent mediators of platelet activation, inflammation and vascular tone. In this paper, the structure of the amine-binding protein (ABP) from Rhodnius prolixus, a vector of the trypanosome that causes Chagas disease, is described. ABP binds the biogenic amines serotonin and norepinephrine with high affinity. A complex with tryptamine shows the presence of a binding site for a single ligand molecule in the central cavity of the beta-barrel structure. The cavity contains significant additional volume, suggesting that this protein may have evolved from the related nitrophorin proteins, which bind a much larger heme ligand in the central cavity.

Structure and ligand-binding properties of the biogenic amine-binding protein from the saliva of a blood-feeding insect vector of Trypanosoma cruzi.,Xu X, Chang BW, Mans BJ, Ribeiro JM, Andersen JF Acta Crystallogr D Biol Crystallogr. 2013 Jan;69(Pt 1):105-13. doi:, 10.1107/S0907444912043326. Epub 2012 Dec 20. PMID:23275168<ref>PMID:23275168</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ge1" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodnius prolixus]]
[[Category: Andersen JF]]
[[Category: Chang BW]]
[[Category: Mans BJ]]
[[Category: Ribeiro JM]]
[[Category: Xu X]]