Crystal structure of RNaseA tandem enzymes and their interaction with the cytosolic ribonuclease inhibitor

• Published in: The FEBS journal Vol. 278; no. 2; p. 331
• Main Authors: Arnold, Ulrich, Leich, Franziska, Neumann, Piotr, Lilie, Hauke, Ulbrich-Hofmann, Renate
• Format: Journal Article
• Language: English
• Published: Oxford Blackwell Publishing Ltd 01.01.2011
• Subjects: Binding sites; Biochemistry; Crystal structure; Enzymes; Molecular biology

Because of their ability to degrade RNA, RNases are potent cytotoxins. The cytotoxic activity of most members of the RNaseA superfamily, however, is abolished by the cytosolic ribonuclease inhibitor (RI). RNaseA tandem enzymes, in which two RNaseA molecules are artificially connected by a peptide li...