PDBsum entry 3eov

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protein Protein-protein interface(s) links
Isomerase/immunosuppressant PDB id
Protein chains
166 a.a. *
11 a.a. *
Waters ×76
* Residue conservation analysis
PDB id:
Name: Isomerase/immunosuppressant
Title: Crystal structure of cyclophilin from leishmania donovani li cyclosporin a
Structure: Peptidyl-prolyl cis-trans isomerase. Chain: a, b. Synonym: ppiase, rotamase, cyclophilin. Engineered: yes. Cyclosporin a. Chain: c, d. Synonym: ciclosporin, ciclosporine. Engineered: yes
Source: Leishmania donovani. Organism_taxid: 5661. Gene: cyp. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Tolypocladium inflatum. Organism_taxid: 29910
2.60Å     R-factor:   0.207     R-free:   0.251
Authors: V.Venugopal,D.Dasgupta,A.K.Datta,R.Banerjee
Key ref: V.Venugopal et al. (2009). Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data. Acta Crystallogr D Biol Crystallogr, 65, 1187-1195. PubMed id: 19923714
29-Sep-08     Release date:   11-Nov-08    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
Q9U9R3  (Q9U9R3_LEIDO) -  Peptidyl-prolyl cis-trans isomerase
187 a.a.
166 a.a.
Protein chains
No UniProt id for this chain
Struc: 11 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.  - Peptidylprolyl isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Peptidylproline (omega=180) = peptidylproline (omega=0)
Peptidylproline (omega=180)
= peptidylproline (omega=0)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     protein folding   2 terms 
  Biochemical function     peptidyl-prolyl cis-trans isomerase activity     1 term  


    Added reference    
Acta Crystallogr D Biol Crystallogr 65:1187-1195 (2009)
PubMed id: 19923714  
Structure of cyclophilin from Leishmania donovani bound to cyclosporin at 2.6 A resolution: correlation between structure and thermodynamic data.
V.Venugopal, A.K.Datta, D.Bhattacharyya, D.Dasgupta, R.Banerjee.
Drug development against Leishmania donovani, the pathogen that causes visceral leishmaniasis in humans, is currently an active area of research given the widespread prevalence of the disease and the emergence of resistant strains. The immunosuppressive drug cyclosporin is known to have antiparasitic activity against a variety of pathogens. The receptor for cyclosporin is the protein cyclophilin, which is a ubiquitous peptidylprolyl isomerase. The crystal structure of cyclophilin from L. donovani complexed with cyclosporin has been solved at 2.6 A resolution. The thermodynamic parameters of the interaction have been determined using spectroscopic and calorimetric techniques. A detailed effort has been made to predict the thermodynamic parameters of binding from computations based on the three-dimensional crystal structure. These results were in good agreement with the corresponding experimental values. Furthermore, the structural and biophysical results have been discussed in the context of leishmanial drug resistance and could also set the stage for the design of potent non-immunosuppressive antileishmanials.