5x6n - Revision history

OCA at 07:28, 7 October 2020

OCA — Wed, 07 Oct 2020 07:28:30 GMT

OCA: Protected "5x6n" [edit=sysop:move=sysop]

OCA — Thu, 09 Mar 2017 16:49:27 GMT

Protected "5x6n" [edit=sysop:move=sysop]

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Revision as of 16:49, 9 March 2017

OCA: New page: ==Structure of P. Knowlesi DBL Domain Capable of binding Human Duffy Antigen== == Structural highlights ==
<table><tr><td colspan='2'>[[5x6n]] is a 1 chain structure. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2c6j 2c6j]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5X6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5X6N FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5x6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5x6n OCA], [http://pdbe.org/5x6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5x6n RCSB], [http://www.ebi.ac.uk/pdbsum/5x6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5x6n ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Molecular processes that govern pathogenic features of erythrocyte invasion and cytoadherence in malaria are reliant on Plasmodium-specific Duffy-binding-like domains (DBLs). These cysteine-rich modules recognize diverse host cell-surface receptors during pathogenesis. DBLs of parasite erythrocyte-binding proteins mediate invasion, and those from the antigenically variant P. falciparum erythrocyte membrane protein 1 (PfEMP1) have been implicated in cytoadherence. The simian and human malarial parasites, P. knowlesi and P. vivax, invade human erythrocytes exclusively through the host DARC receptor (Duffy antigen receptor for chemokines). Here we present the crystal structure of the P. knowlesi DBL domain (Pkalpha-DBL), which binds to DARC during invasion of human erythrocytes. Pkalpha-DBL retains the overall fold observed in DBLs from P. falciparum erythrocyte-binding antigen (EBA)-175 (ref. 4). Mapping the residues that have previously been implicated in binding highlights a fairly flat but exposed site for DARC recognition in subdomain 2 of Pkalpha-DBL; this is in sharp contrast to receptor recognition by EBA-175 (ref. 4). In Pkalpha-DBL, the residues that contact DARC and the clusters of residues under immune pressure map to opposite surfaces of the DBL, and suggest a possible mechanism for immune evasion by P. vivax. Our comparative structural analysis of Pkalpha-DBL and P. falciparum EBA-175 provides a framework for the understanding of malaria parasite DBLs, and may affect the development of new prophylactic and therapeutic strategies.

Structural basis for Duffy recognition by the malaria parasite Duffy-binding-like domain.,Singh SK, Hora R, Belrhali H, Chitnis CE, Sharma A Nature. 2006 Feb 9;439(7077):741-4. Epub 2005 Dec 21. PMID:16372020<ref>PMID:16372020</ref>

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5x6n" style="background-color:#fffaf0;"></div>
== References ==
<references/>
TOC
</StructureSection>
[[Category: Belrhali, H]]
[[Category: Chitnis, C]]
[[Category: Hora, R]]
[[Category: Sharma, A]]
[[Category: Singh, S K]]
[[Category: Cell invasion]]
[[Category: Dbl domain]]
[[Category: Duffy antigen]]
[[Category: P knowlesi]]
[[Category: P vivax]]
[[Category: Receptor]]