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Solution NMR structure of a sheddase inhibitor prodomain from the malarial parasite Plasmodium falciparum
Author(s) -
He Yanan,
Chen Yihong,
Oganesyan Natalia,
Ruan Biao,
O'Brochta David,
Bryan Philip N.,
Orban John
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24187
Subject(s) - plasmodium falciparum , subtilisin , malaria , parasite hosting , plasmodium (life cycle) , homology modeling , protozoa , biology , plasmodium berghei , chemistry , genetics , biochemistry , enzyme , immunology , world wide web , computer science
Plasmodium subtilisin 2 (Sub2) is a multidomain protein that plays an important role in malaria infection. Here, we describe the solution NMR structure of a conserved region of the inhibitory prodomain of Sub2 from Plasmodium falciparum , termed prosub2. Despite the absence of any detectable sequence homology, the protozoan prosub2 has structural similarity to bacterial and mammalian subtilisin‐like prodomains. Comparison with the three‐dimensional structures of these other prodomains suggests a likely binding interface with the catalytic domain of Sub2 and provides insights into the locations of primary and secondary processing sites in Plasmodium prodomains. Proteins 2012;. © 2012 Wiley Periodicals, Inc.