Cyclophilin

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[[Image:2x25.jpg|left|200px|thumb|Crystal Structure of human Cyclophilin-A, [[2x25]]]]
[[Image:2x25.jpg|left|200px|thumb|Crystal Structure of human Cyclophilin-A, [[2x25]]]]
{{STRUCTURE_2x25| PDB=2x25 | SIZE=400| SCENE= |right|CAPTION=human Cyclophilin-A with acetyllysine, [[2x25]] }}
{{STRUCTURE_2x25| PDB=2x25 | SIZE=400| SCENE= |right|CAPTION=human Cyclophilin-A with acetyllysine, [[2x25]] }}
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Revision as of 11:36, 7 March 2013

Image:2x25.jpg
Crystal Structure of human Cyclophilin-A, 2x25

Template:STRUCTURE 2x25










Cyclophilin (Cyp) binds cyclosporin. They are peptidylprolyl isomerases which catalyze the isomerisation of proline. The Cyp-A/cyclosporin A complex inhibits organ rejection. Cyp-D is a component of the mitochondria permeability pore. Rotamase such as FKBP is a prokaryotic Cyp which is not inhibited by cyclosporin but by FK-506 – an immunosuppressive drug. The images at the left and at the right correspond to one representative Cyclophilin, i.e. crystal structure of human Cyclophilin A (2x25).

3D Structures of Cyclophilin

Updated on 07-March-2013

Cyclophilin-A

2x25, 2x2a, 3k0m, 3k0n, 1w8l, 1w8m, 1w8v, 1rmh, 2cpl – hCyp-A – human
1oca – hCyp-A - NMR
3k0o, 3k0p, 3k0q, 3k0r, 2alf – hCyp-A (mutant)
2a2c, 1cwa, 1cwb, 1cwc – hCyp-A+cyclosporin A
3cys - hCyp-A+cyclosporin A - NMR
1cwj, 1bck, 1cwi, 1cwo, 1cwf, 1cwh, 1cwk, 1cwl, 1cwm, 1mik - hCyp-A+cyclosporin A derivative
2rma, 2rmb - hCyp-A+cyclosporin A+cyclosporin A derivative
1mf8, 1m63 - hCyp-A+cyclosporin A+ calcineurin subunits A,B
3odi, 3odl – hCyp-A+voclosporin
2x2d, 1m9c, 1m9d, 1m9e, 1m9f, 1m9x, 1m9y, 1awq, 1awr, 1aws, 1awt, 1awu, 1awv, 1ak4, 1fgl - hCyp-A+HIV-1 N-terminal capsid domain
1zkf – hCyp-A+suc-AGPF-pNA
1ynd, 1nmk – hCyp-A+ sanglifehrin
2cyh, 3cyh, 4cyh, 5cyh - hCyp-A+dipeptide
1vbs, 1vbt – hCyp-A+tetrapeptide
1vdn – yCyp-A+peptidyl coumarin – yeast
1ist – yCyp-A
1w74 – Cyp-A – Mycobacterium tuberculosis
1lop - EcCyp-A+peptidyl nitroanilide - Escherichia coli
1csa – EcCyp-A+ cyclosporin A – NMR
2xgy – Cyp-A+RELIK capsid N-terminal - rabbit
3o7t – NpCyp-A – Noniliophthora perniciosa
3pmp - NpCyp-A + cyclosporin A

Cyclophilin-B

3ich – hCyp-B
3ici - hCyp-B+calmegin fragment
1v9t – EcCyp-B+peptidyl nitroanilide
1vai - EcCyp-B+peptidyl coumarin
1cyn – hCyp-B +cyclosporin A derivative
1j2a – EcCyp-B (mutant)


Cyclophilin-C

2esl - hCyp-C+cyclosporin A
2rmc - Cyp-C+cyclosporin A – mouse


Cyclophilin-D

2bit, 3qyu – hCyp-D
2viu – hCyp-D+DMSO
2z6w - hCyp-D+cyclosporin A


Cyclophilin-E

2kyx, 1zmf – hCyp-E PPIASE domain
2r99 - hCyp-E ABH-like domain
2cqb – hCyp-E RNA recognition motif
2ck1, 2cmt – Cyp-E – Schistosoma mansoni
2kyx – hCyp-E RRM domain – NMR
3lpy, 3mdf - hCyp-E RRM domain


Cyclophilin-G

2wfi, 2gw2 - hCyp-G PPIASE domain
2wfj - hCyp-G PPIASE domain+cyclosporin A


Cyclophilin-H

1mzw – hCyp-H+peptide


Cyclophilin-J

2ok3, 1xyh - hCyp-J
2oju - hCyp-J+cyclosporin A


Cyclophilin-3

2igv, 2igw, 1e8k – CeCyp-3+dipeptide – Caenorhabditis elegans
1dyw - CeCyp-3
1e3b – CeCyp-3+AUP(ET)3


Cyclophilin-5

1h0p – CeCyp-5 (mutant)

Cyclophilin-40

1ihg, 1iip – Cyp-40 – bovine


Cyclophilin

3bo7 - TgCyp+cyclosporin A - Toxoplasma gondii
2nul – EcCyp
1clh – EcCyp – NMR
1qoi – hCyp SNUCYP-20
3k2c – Cyp – Encephalitozoon cuniculi
3eov - LdCyp+cyclosporin A – Leishmania donovani
3bt8 – LdCyp
2haq – LdCyp-A
2hqj – Cyp – Leishmania major
3bkp – TgCyp
2cfe – Cyp – Malassezia sympodialis
2c3b – Cyp – Aspergillus fumigatus
1z81 – Cyp – Plasmodium Yoelli
1qng – PfCyp+cyclosporin A – Plasmodium falciparum
1qnh – PfCyp (mutant)+cyclosporin A
1xo7 – TcCyp – Trypanosoma cruzi
1xq7 - TcCyp+cyclosporin A
1a58 - Cyp – Brugia malayi
2ko7 – BpCyp+inhibitor – Burkholderia pseudomallei
2ke0 – BpCyp – NMR


Rotamase (FKBP)

1fks, 1fkt, 1fkr, 2kfw – EcFKBP – NMR
1q6h, 1q6u – EcFKBP
1q6i – EcFKBP+FK-506
3jxv, 3jym – FKBP73 – wheat
3mdy – hFKBP-1A+BMPR1B
3h9r - hFKBP-1A+ activin receptor type I
1j4r – hFKBP-1+FKB-001
2ppp, 2ppn, 2dg3, 1d6o – hFKBP-12
2ppo – hFKBP-12 (mutant)
2dg4, 1fkb - hFKBP-12+rapamycin
2fap, 1nsg, 1fap - hFKBP-12+rapamycin+FRB
1f40 - hFKBP-12+GPI-1046
1a7x – hFKBP-12+FK-1012
1d7h, 1d7i, 1d7j, 1fkg, 1fkh, 1fki - hFKBP-12+ligand
2dg9 - hFKBP-12 (mutant)+rapamycin
1fkl - cFKBP-12+rapamycin - cow
2pbc - hFKBP-13
1y0o, 1u79 – AtFKBP-13 - Arabidopsis thaliana
2kfv – hFKBP-25 N-terminal
2vn1 – PfFKBP-35 FK506-binding domain+FK506
3b7x – hFKBP-36
2if4 – AtFKBP
2f4e - AtFKBP-42 N-terminal
1kt0, 1kt1 – hFKBP-51 (mutant)
1ix5 – FKBP – Methanothermococcus thermolithotrophicus – NMR
1bl4 – hFKBP (mutant)+inhibitor
1bkf – hFKBP (mutant)+FK-506
1fkf - hFKBP+FK-506
1fkr, 1fks, 1fkt – hFKBP - NMR

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Michal Harel, Alexander Berchansky

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