- The structural basis for catalysis and specificity of the X-prolyl dipeptidyl aminopeptidase from Lactococcus lactisPascal Rigolet
L U R E Centre Universitaire Paris Sud, Bât 209D BP 34, F 91898 Orsay Cedex, France
Structure 10:1383-94. 2002..A C-terminal moiety probably plays a role in the tropism of X-PDAP toward the cellular membrane. These results give new insights for further exploration of the role of the enzymes of the SC clan...
- The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein foldingJie Lin Liu
Laboratoire de Biotechnologies et Pharmacologie Génétique Appliquée CNRS UMR 8113, Ecole Normale Supérieure ENS Cachan, 61 Avenue du President Wilson, 94235 Cachan Cedex, France
J Biol Chem 279:42794-802. 2004..These results revealed that the zinc finger binding motif is involved in maintaining the integrity of the whole protein as well as DNA binding. We also showed that the zinc atom is not essential to enzymatic activity...
- The structural comparison of the bacterial PepX and human DPP-IV reveals sites for the design of inhibitors of PepX activityPascal Rigolet
Laboratoire de Biotechnologies et Pharmacologie Génétique Appliquée CNRS, Ecole Normale Supérieure ENS Cachan, France
FEBS J 272:2050-9. 2005..These results could have applications in human health giving new perspectives to the struggle against pathogens...