Cyclophilin

From Proteopedia

Revision as of 08:08, 17 August 2014

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 17-August-2014

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, 2x2c – 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
4dga, 4dgb, 4dgc - RmCyp-A+HIV-1 Cyp-binding domain capsid protein (mutant) – Rhesus macaque
4dge - RmCyp-A (mutant) +HIV-1 Cyp-binding domain capsid protein (mutant)
4dgd - RmCyp-A (mutant)
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
3rdd – hCyp-A + inhibitor

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
2biu – hCyp-D+DMSO
2z6w - hCyp-D+cyclosporin A
3r49, 3r4g, 3r54, 3r56, 3r57, 3r59, 3rcf, 3rcg, 3rci, 3rck, 3rcl, 3rd9, 3rda, 3rdb, 3rdc, 4j58, 4j59, 4j5a, 4j5b, 4j5c, 4j5d – hCyp-D (mutant) + inhibitor

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