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Single particle raw data of falcilysin in the absence of MK-4815


ABSTRACT:

SUBMITTER: Julien Lescar 

PROVIDER: EMPIAR-13536 | biostudies-other |

REPOSITORIES: biostudies-other

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Inhibition of falcilysin from Plasmodium falciparum by interference with its closed-to-open dynamic transition.

Lin Jianqing J   Yan Xinfu X   Chung Zara Z   Liew Chong Wai CW   El Sahili Abbas A   Pechnikova Evgeniya V EV   Preiser Peter R PR   Bozdech Zbynek Z   Gao Yong-Gui YG   Lescar Julien J  

Communications biology 20240831 1


In the absence of an efficacious vaccine, chemotherapy remains crucial to prevent and treat malaria. Given its key role in haemoglobin degradation, falcilysin constitutes an attractive target. Here, we reveal the mechanism of enzymatic inhibition of falcilysin by MK-4815, an investigational new drug with potent antimalarial activity. Using X-ray crystallography, we determine two binary complexes of falcilysin in a closed state, bound with peptide substrates from the haemoglobin α and β chains re  ...[more]

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