Structures of plasmepsin X from P. falciparum reveal a novel inactivation mechanism of the zymogen a...
Structures of plasmepsin X from P. falciparum reveal a novel inactivation mechanism of the zymogen and molecular basis for binding of inhibitors in mature enzyme
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Author / Creator
Kesari, Pooja , Deshmukh, Anuradha , Pahelkar, Nikhil , Suryawanshi, Abhishek B , Rathore, Ishan , Mishra, Vandana , Dupuis, John H , Xiao, Huogen , Gustchina, Alla , Abendroth, Jan , Labaied, Mehdi , Yada, Rickey Y , Wlodawer, Alexander , Edwards, Thomas E , Lorimer, Donald D and Bhaumik, Prasenjit
Publisher
Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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English
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Cold Spring Harbor: Cold Spring Harbor Laboratory Press
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Contents
Plasmodium falciparum plasmepsin X (PfPMX), involved in the invasion and egress of this deadliest malarial parasite, is essential for its survival and hence considered as an important drug target. We report the first crystal structure of PfPMX zymogen containing a novel fold of its prosegment. A unique twisted loop from the prosegment and arginine...
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Full title
Structures of plasmepsin X from P. falciparum reveal a novel inactivation mechanism of the zymogen and molecular basis for binding of inhibitors in mature enzyme
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TN_cdi_proquest_journals_2576107266
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_2576107266
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E-ISSN
2692-8205
DOI
10.1101/2021.09.24.460453
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https://www.proquest.com/docview/2576107266?pq-origsite=primo&accountid=13902