The structure of human tripeptidyl peptidase II as determined by a hybrid approach.

@article{Schnegge2012TheSO,
  title={The structure of human tripeptidyl peptidase II as determined by a hybrid approach.},
  author={Anne-Marie Sch{\"o}negge and Elizabeth Villa and Friedrich F{\"o}rster and Reiner Hegerl and Juergen Peters and Wolfgang Baumeister and Beate Rockel},
  journal={Structure},
  year={2012},
  volume={20 4},
  pages={593-603}
}
Tripeptidyl-peptidase II (TPPII) is a high molecular mass (∼5 MDa) serine protease, which is thought to act downstream of the 26S proteasome, cleaving peptides released by the latter. Here, the structure of human TPPII (HsTPPII) has been determined to subnanometer resolution by cryoelectron microscopy and single-particle analysis. The complex is built from two strands forming a quasihelical structure harboring a complex system of inner cavities. HsTPPII particles exhibit some polymorphism… CONTINUE READING