Updated on 5 August 2013
"The structure of the Lon protease is so unstable that no enzymatically active Lon protease bound to inhibitors could be crystallized over the past thirty years," Dr. Chang said. "We are happy to be the first team to resolve these complexed structures of Lon isolated from indigenous Taiwanese hot spring bacterium.
This study demonstrates that the crystals of the Lon C protease from indigenous Taiwanese thermophilic bacterium are suitable for inhibitor soaking and consequently structure-based drug design. Importantly, one of the inhibitors whose binding mode was determined is Velcade (bortezomib), a clinically used anti-cancer drug; the result will thus be valuable for design of more specific drugs of this kind with less side effects.