8c44: Difference between revisions

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-'''Unreleased structure'''
-The entry 8c44 is ON HOLD
+==HB3VAR03 apo headstructure (PfEMP1 A) complexed with EPCR==
+<StructureSection load='8c44' size='340' side='right'caption='[[8c44]], [[Resolution|resolution]] 3.20&Aring;' 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]] 3.2&#8491;</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.
-Authors:
+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>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</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]]