8c44: Difference between revisions
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==HB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCR== | |||
<StructureSection load='8c44' size='340' side='right'caption='[[8c44]], [[Resolution|resolution]] 3.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8c44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Plasmodium_falciparum_HB3 Plasmodium falciparum HB3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8C44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8C44 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</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=8c44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8c44 OCA], [https://pdbe.org/8c44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8c44 RCSB], [https://www.ebi.ac.uk/pdbsum/8c44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8c44 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0L7KL67_PLAFX A0A0L7KL67_PLAFX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Severe Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands. Using cryogenic electron microscopy (Cryo-EM) and PfEMP1 sequence diversity analysis, we found that group A PfEMP1 CIDRalpha1 domains interact with the adjacent DBLalpha1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLalpha1 domain is displaced, and the EPCR-binding helix of CIDRalpha1 is turned, kinked, and twisted to reach a rearranged, stable EPCR-bound conformation. The unbound conformation and the required transition to the EPCR-bound conformation may represent a conformational masking mechanism of immune evasion for the PfEMP1 family. | |||
Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1.,Rajan Raghavan SS, Turner L, Jensen RW, Johansen NT, Jensen DS, Gourdon P, Zhang J, Wang Y, Theander TG, Wang K, Lavstsen T Structure. 2023 Oct 5;31(10):1174-1183.e4. doi: 10.1016/j.str.2023.07.011. Epub , 2023 Aug 14. PMID:37582356<ref>PMID:37582356</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8c44" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Plasmodium falciparum HB3]] | |||
[[Category: Lavstsen T]] | |||
[[Category: Raghavan SSR]] | |||
[[Category: Wang KT]] | |||
Latest revision as of 14:58, 23 October 2024
HB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCRHB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCR
Structural highlights
FunctionPublication Abstract from PubMedSevere Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands. Using cryogenic electron microscopy (Cryo-EM) and PfEMP1 sequence diversity analysis, we found that group A PfEMP1 CIDRalpha1 domains interact with the adjacent DBLalpha1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLalpha1 domain is displaced, and the EPCR-binding helix of CIDRalpha1 is turned, kinked, and twisted to reach a rearranged, stable EPCR-bound conformation. The unbound conformation and the required transition to the EPCR-bound conformation may represent a conformational masking mechanism of immune evasion for the PfEMP1 family. Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1.,Rajan Raghavan SS, Turner L, Jensen RW, Johansen NT, Jensen DS, Gourdon P, Zhang J, Wang Y, Theander TG, Wang K, Lavstsen T Structure. 2023 Oct 5;31(10):1174-1183.e4. doi: 10.1016/j.str.2023.07.011. Epub , 2023 Aug 14. PMID:37582356[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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