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==Merozoite surface protein 1 (MSP-1) from Plasmodium falciparum, alternative conformation 4==
<StructureSection load='6zbg' size='340' side='right'caption='[[6zbg]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6zbg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum Plasmodium falciparum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZBG 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6zbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6zbg OCA], [https://pdbe.org/6zbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6zbg RCSB], [https://www.ebi.ac.uk/pdbsum/6zbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6zbg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q25922_PLAFA Q25922_PLAFA] By binding to host proinflammatory cytokine S100P may interfere with host immune responses.[ARBA:ARBA00043850]
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== Publication Abstract from PubMed ==
The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading Plasmodium merozoite, the causative agent of malaria. MSP-1 is essential for merozoite formation, entry into and escape from erythrocytes, and is a promising vaccine candidate. Here, we present monomeric and dimeric structures of full-length MSP-1. MSP-1 adopts an unusual fold with a large central cavity. Its fold includes several coiled-coils and shows structural homology to proteins associated with membrane and cytoskeleton interactions. MSP-1 formed dimers through these domains in a concentration-dependent manner. Dimerization is affected by the presence of the erythrocyte cytoskeleton protein spectrin, which may compete for the dimerization interface. Our work provides structural insights into the possible mode of interaction of MSP-1 with erythrocytes and establishes a framework for future investigations into the role of MSP-1 in Plasmodium infection and immunity.

Structure of the merozoite surface protein 1 from Plasmodium falciparum.,Dijkman PM, Marzluf T, Zhang Y, Chang SS, Helm D, Lanzer M, Bujard H, Kudryashev M Sci Adv. 2021 Jun 2;7(23):eabg0465. doi: 10.1126/sciadv.abg0465. Print 2021 Jun. PMID:34078606<ref>PMID:34078606</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6zbg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Plasmodium falciparum]]
[[Category: Dijkman PM]]
[[Category: Kudryashev M]]