View source for 4bik


==Structure of a disulfide locked mutant of Intermedilysin with human CD59==
<StructureSection load='4bik' size='340' side='right'caption='[[4bik]], [[Resolution|resolution]] 3.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bik]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Streptococcus_intermedius Streptococcus intermedius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BIK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BIK 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]] 3.494&#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=4bik FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bik OCA], [https://pdbe.org/4bik PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bik RCSB], [https://www.ebi.ac.uk/pdbsum/4bik PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bik ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9LCB8_STRIT Q9LCB8_STRIT] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Pore-forming proteins containing the structurally conserved membrane attack complex/perforin fold play an important role in immunity and host-pathogen interactions. Intermedilysin (ILY) is an archetypal member of a cholesterol-dependent cytolysin subclass that hijacks the complement receptor CD59 to make cytotoxic pores in human cells. ILY directly competes for the membrane attack complex binding site on CD59, rendering cells susceptible to complement lysis. To understand how these bacterial pores form in lipid bilayers and the role CD59 plays in complement regulation, we determined the crystal structure of human CD59 bound to ILY. Here, we show the ILY-CD59 complex at 3.5 A resolution and identify two interfaces mediating this host-pathogen interaction. An ILY-derived peptide based on the binding site inhibits pore formation in a CD59-containing liposome model system. These data provide insight into how CD59 coordinates ILY monomers, nucleating an early prepore state, and suggest a potential mechanism of inhibition for the complement terminal pathway.

Structural Basis for Recognition of the Pore-Forming Toxin Intermedilysin by Human Complement Receptor CD59.,Johnson S, Brooks NJ, Smith RA, Lea SM, Bubeck D Cell Rep. 2013 May 30;3(5):1369-77. doi: 10.1016/j.celrep.2013.04.029. Epub 2013 , May 9. PMID:23665225<ref>PMID:23665225</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bik" style="background-color:#fffaf0;"></div>

==See Also==
*[[CD59|CD59]]
*[[Cytolysin 3D structures|Cytolysin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Streptococcus intermedius]]
[[Category: Brooks NJ]]
[[Category: Bubeck D]]
[[Category: Johnson S]]
[[Category: Lea SM]]
[[Category: Smith RAG]]