View source for 7pi6


==Trypanosoma brucei ISG65 bound to human complement C3d==
<StructureSection load='7pi6' size='340' side='right'caption='[[7pi6]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7pi6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Trypanosoma_brucei_brucei_TREU927 Trypanosoma brucei brucei TREU927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PI6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PI6 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]] 2.6&#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=PG0:2-(2-METHOXYETHOXY)ETHANOL'>PG0</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=7pi6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pi6 OCA], [https://pdbe.org/7pi6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pi6 RCSB], [https://www.ebi.ac.uk/pdbsum/7pi6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pi6 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
African trypanosomes are extracellular pathogens of mammals and are exposed to the adaptive and innate immune systems. Trypanosomes evade the adaptive immune response through antigenic variation, but little is known about how they interact with components of the innate immune response, including complement. Here we demonstrate that an invariant surface glycoprotein, ISG65, is a receptor for complement component 3 (C3). We show how ISG65 binds to the thioester domain of C3b. We also show that C3 contributes to control of trypanosomes during early infection in a mouse model and provide evidence that ISG65 is involved in reducing trypanosome susceptibility to C3-mediated clearance. Deposition of C3b on pathogen surfaces, such as trypanosomes, is a central point in activation of the complement system. In ISG65, trypanosomes have evolved a C3 receptor which diminishes the downstream effects of C3 deposition on the control of infection.

Invariant surface glycoprotein 65 of Trypanosoma brucei is a complement C3 receptor.,Macleod OJS, Cook AD, Webb H, Crow M, Burns R, Redpath M, Seisenberger S, Trevor CE, Peacock L, Schwede A, Kimblin N, Francisco AF, Pepperl J, Rust S, Voorheis P, Gibson W, Taylor MC, Higgins MK, Carrington M Nat Commun. 2022 Aug 29;13(1):5085. doi: 10.1038/s41467-022-32728-9. PMID:36038546<ref>PMID:36038546</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7pi6" style="background-color:#fffaf0;"></div>

==See Also==
*[[Complement C3 3D structures|Complement C3 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Trypanosoma brucei brucei TREU927]]
[[Category: Cook AD]]
[[Category: Higgins MK]]