Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 80, Issue 12, Pages 2810-2817Publisher
WILEY
DOI: 10.1002/prot.24187
Keywords
malaria; Plasmodium; subtilisin; protease; sheddase; prodomain; structure; NMR; therapeutics
Categories
Funding
- Bill and Melinda Gates Foundation
- University of Maryland Seed Grant Program
- W. M. Keck Foundation
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available