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. Author manuscript; available in PMC: 2016 Jan 29.
Published in final edited form as: Science. 2014 Feb 27;343(6176):1244–1248. doi: 10.1126/science.1249845

Fig. 2. KH and KEN homodimers.

Fig. 2

(A) Symmetrical salt bridges stabilize the interfaces between the KH (1364 Å2) and RNase (943 Å2) domains. Mutations of these salt bridges impair RNase L activity. (B) Comparison of KEN domains in RNase L and Ire1. Key active-site residues are indicated. (C) Effect of HLE mutagenesis on cleavage of ssRNA and RNA hairpins derived from human XBP1 mRNA. WC indicates the number of Watson-Crick base pairs in the hairpin stem. Ire1KR32 is yeast Ire1 kinase/RNase. Reactions contained 100 nM Ire1KR32 and 5 nM RNase L. Error bars show mean ± SE.