Structural insights into substrate binding by PvFKBP35, a peptidylprolyl cis-trans isomerase from the human malarial parasite plasmodium vivax

• Main Authors: Alag, Reema, Balakrishna, Asha Manikkoth, Rajan, Sreekanth, Qureshi, Insaf A., Shin, Joon, Lescar, Julien, Grüber, Gerhard, Yoon, Ho Sup
• Other Authors: School of Biological Sciences
• Format: Article
• Language: English
• Published: 2015
• Subjects: DRNTU::Science::Biological sciences
• Online Access: https://hdl.handle.net/10356/106116; http://hdl.handle.net/10220/26349
• Institution: Nanyang Technological University

The immunosuppressive drug FK506 binding proteins (FKBPs), an immunophilin family with the immunosuppressive drug FK506 binding property, exhibit peptidylprolyl cis-trans isomerase (PPIase) activity. While the cyclophilin-catalyzed peptidylprolyl isomerization of X-Pro peptide bonds has been extensi...