Pertussis Toxin-ATP Complex: Difference between revisions

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 ==Conclusion==
-This paper was significant since it gave a clear understanding of the PT activation as well as a better understanding to the pathogenesis of the toxin. The key features of this proposal is that ATP binding signals the arrival of the PT in the endoplasmic reticulum by acting as a molecular sensor.<ref name=Hazes>PMID: 8637000</ref> This detection of the PT in the ER at the same time triggers dissociation of the holotoxin prior to membrane translocation.<ref name=Hazes>PMID: 8637000</ref> Therefore, the dissociation is due to ATP binding destabilization and reduction by protein disulphide isomerase.<ref name=Hazes>PMID: 8637000</ref>
+The findings of PT activation was significant since it illustrated a better understanding for the pathogenesis of the toxin. The key features of this proposal is that ATP binding signals the arrival of the PT in the endoplasmic reticulum by acting as a molecular sensor.<ref name=Hazes>PMID: 8637000</ref> This detection of the PT in the ER at the same time triggers dissociation of the holotoxin prior to membrane translocation.<ref name=Hazes>PMID: 8637000</ref> Therefore, the dissociation is due to ATP binding destabilization, reduction by protein disulphide isomerase, and proteolytic cleavage.<ref name=Hazes>PMID: 8637000</ref>
 </StructureSection>
+==3D structures of Pertussis toxin==
+[[Pertussis toxin]]
 ==References==
 <references/>