Solution structural analysis of the single-domain parvulin TbPin1.

ABSTRACT:

Background

Pin1-type parvulins are phosphorylation-dependent peptidyl-prolyl cis-trans isomerases. Their functions have been widely reported to be involved in a variety of cellular responses or processes, such as cell division, transcription, and apoptosis, as well as in human diseases including Alzheimer's disease and cancers. TbPin1 was identified as a novel class of Pin1-type parvulins from Trypanosoma brucei, containing a unique PPIase domain, which can catalyze the isomerization of phosphorylated Ser/Thr-Pro peptide bond.

Methodology/principal findings

We determined the solution structure of TbPin1 and performed (15)N relaxation measurements to analyze its backbone dynamics using multi-dimensional heteronuclear NMR spectroscopy. The average RMSD values of the 20 lowest

SUBMITTER: Sun L 

PROVIDER: S-EPMC3416822 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature