structural basis for specificity of propeptide-enzyme interaction in barley c1a cysteine peptidases特异性结构依据propeptide-enzyme交互的大麦c1a半胱氨酸肽酶.pdf

Structural Basis for Specificity of Propeptide-Enzyme Interaction in Barley C1A Cysteine Peptidases ´ ´ Ines Cambra, David Hernandez, Isabel Diaz, Manuel Martinez* ´ ´ ´ ´ Centro de Biotecnologıa y Genomica de Plantas, Universidad Politecnica de Madrid, Pozuelo de Alarcon, Madrid, Spain Abstract C1A cysteine peptidases are synthesized as inactive proenzymes. Activation takes place by proteolysis cleaving off the inhibitory propeptide. The inhibitory capacity of propeptides from barley cathepsin L and B-like peptidases towards commercial and barley cathepsins has been characterized. Differences in selectivity have been found for propeptides from L-cathepsins against their cognate and non cognate enzymes. Besides, the propeptide from barley cathepsin B was not able to inhibit bovine cathepsin B. Modelling of their three-dimensional structures suggests that most propeptide inhibitory properties can be explained from the interaction between the propeptide and the mature cathepsin structures. Their potential use as biotechnological tools is discussed. ´ Citation: Cambra I, Hernandez D, Diaz I, Martinez M (2012) Structural Basis for Specificity of Propeptide-Enzyme Interaction in Barley C1A Cysteine Peptidases. PLoS ONE 7(5): e37234. doi:10.1371/journal.pone.0037234 Editor: Guy Smagghe, Ghent University, Belgium Received October 7, 2011; Accepted April 18, 2012; Published May 17, 2012 Copyright: 2012 Cambra et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided th