PDBsum entry 2rmc

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protein Protein-protein interface(s) links
Isomerase/immunosuppressant PDB id
Protein chains
182 a.a. *
11 a.a. *
Waters ×1203
* Residue conservation analysis
PDB id:
Name: Isomerase/immunosuppressant
Title: Crystal structure of murine cyclophilin c complexed with immunosuppressive drug cyclosporin a
Structure: Peptidyl-prolyl cis-trans isomerasE C. Chain: a, c, e, g. Synonym: rotamasE C, cyclophilin c. Engineered: yes. Cyclosporin a. Chain: b, d, f, h. Synonym: ciclosporin, ciclosporine. Engineered: yes
Source: Mus musculus. Organism_taxid: 10090. Synthetic: yes. Tolypocladium inflatum. Organism_taxid: 29910
Biol. unit: Octamer (from PQS)
1.64Å     R-factor:   0.197    
Authors: H.Ke,Y.Zhao,F.Luo,I.Weissman,J.Friedman
Key ref: H.Ke et al. (1993). Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A. Proc Natl Acad Sci U S A, 90, 11850-11854. PubMed id: 8265636
07-Jan-94     Release date:   14-Feb-95    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P30412  (PPIC_MOUSE) -  Peptidyl-prolyl cis-trans isomerase C
212 a.a.
182 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, C, E, G: 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    
Proc Natl Acad Sci U S A 90:11850-11854 (1993)
PubMed id: 8265636  
Crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A.
H.Ke, Y.Zhao, F.Luo, I.Weissman, J.Friedman.
Cyclophilin is a cellular receptor for the immunosuppressive drug cyclosporin A (CsA). Cyclophilin C (CyPC) is highly expressed in murine kidney, making it a potential mediator of the nephrotoxic effects of CsA. The structure of murine CyPC complexed with CsA has been solved and refined to an R factor of 0.197 at a 1.64-A resolution. Superposition of the CyPC-CsA structure with the unligated cyclophilin A (CyPA) revealed significant migration of three loops: Gln-179 to Thr-189, Asp-47 to Lys-49, and Met-170 to Ile-176. The proximity of the loop Gln-179 to Thr-189 to the CsA binding site may account for the unique binding of a 77-kDa glycoprotein, CyPC binding protein (CyCAP), to CyPC. The binding of CsA to CyPC is similar to that of CsA to human T-cell cyclophilin A (CyPA). However, the conformation of CsA when bound to CyPC is significantly different from that when bound to CyPA. These differences may reflect conformational variation of CsA when bound to different proteins. Alternatively, the previous CyPA-CsA structure at low resolution may not provide sufficient details for a comparison with the CyPC-CsA structure.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18385230 F.Yang, J.M.Robotham, H.B.Nelson, A.Irsigler, R.Kenworthy, and H.Tang (2008).
Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro.
  J Virol, 82, 5269-5278.  
17414949 K.Kitahara, and S.Kawai (2007).
Cyclosporine and tacrolimus for the treatment of rheumatoid arthritis.
  Curr Opin Rheumatol, 19, 238-245.  
17225137 P.Mark, and L.Nilsson (2007).
A molecular dynamics study of Cyclophilin A free and in complex with the Ala-Pro dipeptide.
  Eur Biophys J, 36, 213-224.  
15735342 L.L.Huang, X.M.Zhao, C.Q.Huang, L.Yu, and Z.X.Xia (2005).
Structure of recombinant human cyclophilin J, a novel member of the cyclophilin family.
  Acta Crystallogr D Biol Crystallogr, 61, 316-321.
PDB code: 1xyh
15998457 P.Wang, and J.Heitman (2005).
The cyclophilins.
  Genome Biol, 6, 226.  
11592084 K.Jalkanen, T.Leu, P.Bono, M.Salmi, S.Jalkanen, and D.J.Smith (2001).
Distinct ligand binding properties of Mac-2-binding protein and mouse cyclophilin [correction of mousephilin] C-associated protein.
  Eur J Immunol, 31, 3075-3084.  
  11206060 M.Carpentier, F.Allain, B.Haendler, M.C.Slomianny, and G.Spik (2000).
Delineation of the calcineurin-interacting region of cyclophilin B.
  Protein Sci, 9, 2386-2393.  
11058892 M.T.Ivery (2000).
Immunophilins: switched on protein binding domains?
  Med Res Rev, 20, 452-484.  
10642184 P.J.Ellis, C.K.Carlow, D.Ma, and P.Kuhn (2000).
Crystal structure of the complex of brugia malayi cyclophilin and cyclosporin A.
  Biochemistry, 39, 592-598.
PDB codes: 1c5f 1qtl
  10422840 R.Golbik, G.Fischer, and A.R.Fersht (1999).
Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18).
  Protein Sci, 8, 1505-1514.  
  9655334 V.Mikol, D.Ma, and C.K.Carlow (1998).
Crystal structure of the cyclophilin-like domain from the parasitic nematode Brugia malayi.
  Protein Sci, 7, 1310-1316.
PDB code: 1a33
  9385632 F.F.Vajdos, S.Yoo, M.Houseweart, W.I.Sundquist, and C.P.Hill (1997).
Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.
  Protein Sci, 6, 2297-2307.
PDB codes: 1awq 1awr 1aws 1awt 1awu 1awv
8652511 Y.Zhao, and H.Ke (1996).
Crystal structure implies that cyclophilin predominantly catalyzes the trans to cis isomerization.
  Biochemistry, 35, 7356-7361.
PDB code: 1rmh
8652512 Y.Zhao, and H.Ke (1996).
Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes.
  Biochemistry, 35, 7362-7368.
PDB codes: 2cyh 3cyh 4cyh 5cyh
  8559592 H.C.Roberts, J.M.Sternberg, and L.H.Chappell (1995).
Hymenolepis diminuta and H. microstoma: uptake of cyclosporin A and drug binding to parasite cyclophilins.
  Parasitology, 111, 591-597.  
7866747 D.Altschuh, W.Braun, J.Kallen, V.Mikol, C.Spitzfaden, J.C.Thierry, O.Vix, M.D.Walkinshaw, and K.Wüthrich (1994).
Conformational polymorphism of cyclosporin A.
  Structure, 2, 963-972.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.