2LJ4

Solution structure of the TbPIN1

Summary for 2LJ4

• Entry DOI: 10.2210/pdb2lj4/pdb
• NMR Information: BMRB: 17918
• Descriptor: Peptidyl-prolyl cis-trans isomerase/rotamase, putative (1 entity in total)
• Functional Keywords: tbpin1, isomerase
• Biological source: Trypanosoma brucei
• Total number of polymer chains: 1
• Total formula weight: 12515.03

Authors

Sun, L.,Lin, D.,Zhao, Y. (deposition date: 2011-09-06, release date: 2012-08-22, Last modification date: 2024-05-15)

Primary citation

Sun, L.,Wu, X.,Peng, Y.,Goh, J.Y.,Liou, Y.-C.,Lin, D.,Zhao, Y.
Solution structural analysis of the single-domain parvulin TbPin1.
Plos One, 7:e43017-e43017, 2012

PubMed Abstract: 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.

PubMed: 22900083
DOI: 10.1371/journal.pone.0043017

Experimental method

SOLUTION NMR