High-resolution crystal structure of the leucine-rich repeat domain of the human tumour suppressor PP32A (ANP32A).

ABSTRACT: Acidic leucine-rich nuclear phosphoprotein 32A (PP32A) is a tumour suppressor whose expression is altered in many cancers. It is an apoptotic enhancer that stimulates apoptosome-mediated caspase activation and also forms part of a complex involved in caspase-independent apoptosis (the SET complex). Crystals of a fragment of human PP32A corresponding to the leucine-rich repeat domain, a widespread motif suitable for protein-protein interactions, have been obtained. The structure has been refined to 1.56 Å resolution. This domain was previously solved at 2.4 and 2.69 Å resolution (PDB entries 2je0 and 2je1, respectively). The new high-resolution structure shows some differences from previous models: there is a small displacement in the turn connecting the first α-helix (α1) to the first β-st

SUBMITTER: Zamora-Caballero S 

PROVIDER: S-EPMC4461331 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature