Cryo-EM structure of Nma111p, a unique HtrA protease composed of two protease domains and four PDZ domains
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Dear Editor,Apoptosis,a physiological form of programmed cell death,is essential for the maintenance of normal cellular homeostasis ”1”.In the unicellular eukaryote Saccharomyces cerevisiae,a number of evolutionarily conserved apoptosis-regulatory proteins have been identified,one of which is nuclear mediator of apoptosis 111 kDa protein (Nma111p),a protease targeting Birlp,the sole inhibitor-of-apoptosis protein (IAP) in yeast ”2”.Nma111p is a serine protease of the HtrA family,of which a common structural feature is the presence of the trypsin-like protease domain and the post-synaptic density 95,Drosophila discs large,zona-occludens-1 (PDZ) domain ”3”.
Saccharomyces cerevisiae、programmed cell death、structural feature、serine protease、form of
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X1 ;TS2
This work was funded by grants from the National Natural Science Foundation of China31230016/31370717;the National Basic Research Program of China2016YFA0501101;by Tsinghua-Peking Joint Center for Life Sciences,Advanced Innovation Center for Structural Biology and One-Thousand Talent Program of China