Title : Tetrameric
dipeptidyl peptidase I directs substrate specificity by use of the residual
pro-part
domain
Abstract :
- The crystal structure of mature dipeptidyl peptidase I reveals insight into the unique tetrameric structure, substrate binding and activation of this atypical papain family peptidase
- Each subunit is composed of three peptides
- The heavy and light chains form the catalytic domain , which adopts the papain fold
- The residual pro-part forms a beta-barrel with the carboxylate group of Asp1 pointing towards the substrate amino-terminus
- The tetrameric structure appears to stabilize the association of the two domains and encloses a 12700 A3 spherical cavity
- The tetramer contains six chloride ions, one buried in each S2 pocket and two at subunit interfaces