Structural insights into substrate binding by PvFKBP35, a peptidylprolyl cis-trans isomerase from the human malarial parasite plasmodium vivax
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...
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: | Journal Article |
Language: | English |
Published: |
2015
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/106116 http://hdl.handle.net/10220/26349 |
Similar Items
-
NMR and crystallographic structures of the FK506 binding domain of human malarial parasite Plasmodium vivax FKBP35
by: Alag, Reema, et al.
Published: (2012) -
Molecular characterization of plasmodium vivax FK506-binding protein 25 (PvFKBP25).
by: Quah, Yee Wen.
Published: (2013) -
Structural and biochemical characterization of FK506 binding protein (FKBP) from plasmodium falciparum any) plasmodium vivax.
by: Reema Alag
Published: (2014) -
NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax
by: Shin, Joon, et al.
Published: (2012) -
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD
by: Quistgaard, Esben M., et al.
Published: (2016)