This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Cyclophilin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:57, 22 May 2019) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
 +
<StructureSection load='2x2c' size='350' side='right' caption='Human Cyclophilin-A (rust, olive, turquois, dark green, khaki) complex with cyclosporin A (green, cyan, aqua, neon green, blue) (PDB entry [[2x2c]])' scene='41/415818/Cv/1'>
 +
== Function ==
 +
[[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. <ref>PMID:14731520</ref> See also [[Isomerases]].
-
<StructureSection load='2x25' size='350' side='right' caption='Human Cyclophilin-A with acetyllysine (PDB entry [[2x25]])' scene=''>
+
== Relevance ==
-
[[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. <ref>PMID:11742345</ref>
+
Cyp-A has a key role in immunosuppression and viral infection<ref>PMID:22814107</ref>. Cyp-A is the target of the immunosuppressant cyclosporin A whose binding leads to the suppression of the T-cell mediated immune response. Cyp-A is required for effective HIV-1 replication in host cells<ref>PMID:15596813</ref>.
-
</StructureSection>
+
-
== 3D Structures of Cyclophilin ==
+
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
== Structural highlights ==
-
{{#tree:id=OrganizedByTopic|openlevels=0|
+
-
* Cyclophilin-A
+
<scene name='41/415818/Cv/2'>Cyp-A undergoes post-translational acetylation of Lys125</scene>. The acetylation modulates key functions of Cyp-A activity.<ref>PMID:20364129</ref>
-
**[[2x25]], [[2x2a]], [[3k0m]], [[3k0n]], [[1w8l]], [[1w8m]], [[1w8v]], [[1rmh]], [[2cpl]] – hCyp-A – human<br />
+
== 3D Structures of Cyclophilin ==
-
**[[1oca]] – hCyp-A - NMR<br />
+
[[Cyclophilin 3D structures]]
-
**[[3k0o]], [[3k0p]], [[3k0q]], [[3k0r]], [[2alf]] – hCyp-A (mutant)<br />
+
-
**[[4dgd]] - RmCyp-A (mutant) – Rhesus macaque <br />
+
-
**[[1ist]] – yCyp-A – yeast<br />
+
-
**[[1w74]] – Cyp-A – ''Mycobacterium tuberculosis''<br />
+
-
**[[3o7t]] – NpCyp-A – ''Noniliophthora perniciosa''<br />
+
-
**[[4e1q]] – Cyp-A – wheat<br />
+
-
**[[4eyv]] – Cyp-A – ''Piriformospora indica''<br />
+
-
* Cyclophilin-A complex
+
</StructureSection>
-
 
+
-
**[[2a2c]], [[1cwa]], [[1cwb]], [[1cwc]], [[2x2c]] – hCyp-A+cyclosporin A<br />
+
-
**[[3cys]] - hCyp-A+cyclosporin A - NMR<br />
+
-
**[[1cwj]], [[1bck]], [[1cwi]], [[1cwo]], [[1cwf]], [[1cwh]], [[1cwk]], [[1cwl]], [[1cwm]], [[1mik]] - hCyp-A+cyclosporin A derivative<br />
+
-
**[[2rma]], [[2rmb]] - hCyp-A+cyclosporin A+cyclosporin A derivative<br />
+
-
**[[1mf8]], [[1m63]] - hCyp-A+cyclosporin A+ calcineurin subunits A,B<br />
+
-
**[[3odi]], [[3odl]] – hCyp-A+voclosporin<br />
+
-
**[[2x2d]], [[1m9c]], [[1m9d]], [[1m9e]], [[1m9f]], [[1m9x]], [[1m9y]], [[1awq]], [[1awr]], [[1aws]], [[1awt]], [[1awu]], [[1awv]], [[1ak4]], [[1fgl]] - hCyp-A+HIV-1 N-terminal capsid domain<br />
+
-
**[[4dga]], [[4dgb]], [[4dgc]] - RmCyp-A+HIV-1 Cyp-binding domain capsid protein (mutant) <br />
+
-
**[[4dge]] - RmCyp-A (mutant) +HIV-1 Cyp-binding domain capsid protein (mutant) <br />
+
-
**[[1zkf]] – hCyp-A+suc-AGPF-pNA<br />
+
-
**[[1ynd]], [[1nmk]] – hCyp-A+ sanglifehrin<br />
+
-
**[[2cyh]], [[3cyh]], [[4cyh]], [[5cyh]] - hCyp-A+dipeptide<br />
+
-
**[[1vbs]], [[1vbt]] – hCyp-A+tetrapeptide<br />
+
-
**[[1vdn]] – yCyp-A+peptidyl coumarin – yeast<br />
+
-
**[[1lop]] - EcCyp-A+peptidyl nitroanilide - ''Escherichia coli''<br />
+
-
**[[1csa]] – EcCyp-A+ cyclosporin A – NMR<br />
+
-
**[[2xgy]] – Cyp-A+RELIK capsid N-terminal - rabbit<br />
+
-
**[[3o7t]] – NpCyp-A – ''Noniliophthora perniciosa''<br />
+
-
**[[3pmp]] - NpCyp-A + cyclosporin A<br />
+
-
**[[3rdd]] – hCyp-A + inhibitor<br />
+
-
**[[3t1u]] – Cyp-A + peptide – ''Azotobacter vinelandii''<br />
+
-
 
+
-
* Cyclophilin-B
+
-
 
+
-
**[[3ich]] – hCyp-B<br />
+
-
**[[3ici]] - hCyp-B+calmegin fragment<br />
+
-
**[[1v9t]] – EcCyp-B+peptidyl nitroanilide <br />
+
-
**[[1vai]] - EcCyp-B+peptidyl coumarin<br />
+
-
**[[1cyn]] – hCyp-B +cyclosporin A derivative<br />
+
-
**[[2rs4]] – EcCyp-B - NMR<BR />
+
-
**[[1j2a]] – EcCyp-B (mutant)<br />
+
-
**[[4fru]] – hoCyp-B – horse<br />
+
-
**[[4frv]] – hoCyp-B (mutant)<br />
+
-
**[[1a58]], [[4jcp]] – Cyp-B – ''Brugia malayi''<br />
+
-
 
+
-
* Cyclophilin-C
+
-
 
+
-
**[[2esl]] - hCyp-C+cyclosporin A<br />
+
-
**[[2rmc]] - Cyp-C+cyclosporin A – mouse<br />
+
-
**[[1jns]], [[1jnt]] – EcCyp-C - NMR<BR />
+
-
 
+
-
* Cyclophilin-D
+
-
 
+
-
**[[2bit]], [[3qyu]] – hCyp-D<br />
+
-
**[[2biu]] – hCyp-D+DMSO<br />
+
-
**[[2z6w]] - hCyp-D+cyclosporin A<br />
+
-
**[[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<br />
+
-
 
+
-
* Cyclophilin-E
+
-
 
+
-
**[[2kyx]], [[1zmf]] – hCyp-E PPIASE domain<br />
+
-
**[[2r99]] - hCyp-E ABH-like domain<br />
+
-
**[[2cqb]] – hCyp-E RNA recognition motif<br />
+
-
**[[2ck1]], [[2cmt]] – Cyp-E – ''Schistosoma mansoni''<br />
+
-
**[[2kyx]] – hCyp-E RRM domain – NMR<br />
+
-
**[[3lpy]], [[3mdf]] - hCyp-E RRM domain<br />
+
-
 
+
-
* Cyclophilin-G
+
-
 
+
-
**[[2wfi]], [[2gw2]] - hCyp-G PPIASE domain<br />
+
-
**[[2wfj]] - hCyp-G PPIASE domain+cyclosporin A<br />
+
-
 
+
-
* Cyclophilin-H
+
-
 
+
-
**[[1mzw]] – hCyp-H+peptide<br />
+
-
 
+
-
* Cyclophilin-J
+
-
 
+
-
**[[2ok3]], [[1xyh]] - hCyp-J<br />
+
-
**[[2oju]] - hCyp-J+cyclosporin A<br />
+
-
 
+
-
* Cyclophilin-3
+
-
 
+
-
**[[2igv]], [[2igw]], [[1e8k]] – CeCyp-3+dipeptide – ''Caenorhabditis elegans''<br />
+
-
**[[1dyw]] - CeCyp-3<br />
+
-
**[[1e3b]] – CeCyp-3+AUP(ET)3<br />
+
-
 
+
-
* Cyclophilin-5
+
-
 
+
-
**[[1h0p]] – CeCyp-5 (mutant) <br />
+
-
 
+
-
* Cyclophilin-38
+
-
 
+
-
**[[3rfy]] – Cyp-38 – ''Arabidopsis thaliana''<br />
+
-
 
+
-
* Cyclophilin-40
+
-
 
+
-
**[[1ihg]], [[1iip]] – Cyp-40 – bovine<br />
+
-
 
+
-
* Cyclophilin
+
-
**[[3bo7]] - TgCyp+cyclosporin A - ''Toxoplasma gondii''<br />
 
-
**[[2nul]] – EcCyp<br />
 
-
**[[1clh]] – EcCyp – NMR<br />
 
-
**[[1qoi]] – hCyp SNUCYP-20<br />
 
-
**[[3k2c]] – Cyp – ''Encephalitozoon cuniculi''<br />
 
-
**[[3eov]] - LdCyp+cyclosporin A – ''Leishmania donovani''<br />
 
-
**[[3bt8]] – LdCyp<br />
 
-
**[[2haq]] – LdCyp-A<br />
 
-
**[[2hqj]] – Cyp – ''Leishmania major''<br />
 
-
**[[3bkp]] – TgCyp<br />
 
-
**[[2cfe]] – Cyp – ''Malassezia sympodialis''<br />
 
-
**[[2c3b]] – Cyp – ''Aspergillus fumigatus''<br />
 
-
**[[1z81]] – Cyp – ''Plasmodium Yoelli''<br />
 
-
**[[1qng]] – PfCyp+cyclosporin A – ''Plasmodium falciparum''<br />
 
-
**[[1qnh]] – PfCyp (mutant)+cyclosporin A<br />
 
-
**[[1xo7]] – TcCyp – ''Trypanosoma cruzi''<br />
 
-
**[[1xq7]] - TcCyp+cyclosporin A<br />
 
-
**[[2ko7]], [[2l2s]] – BpCyp+inhibitor – ''Burkholderia pseudomallei''<br />
 
-
**[[2ke0]], [[3s6m]] – BpCyp – NMR<br />
 
-
**[[4dz2]], [[4dz3]] – BpPin1 (mutant) + FK506<BR />
 
-
}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Human Cyclophilin-A (rust, olive, turquois, dark green, khaki) complex with cyclosporin A (green, cyan, aqua, neon green, blue) (PDB entry 2x2c)

Drag the structure with the mouse to rotate

References

  1. ↑ Stamnes MA, Rutherford SL, Zuker CS. Cyclophilins: a new family of proteins involved in intracellular folding. Trends Cell Biol. 1992 Sep;2(9):272-6. PMID:14731520
  2. ↑ Zhou D, Mei Q, Li J, He H. Cyclophilin A and viral infections. Biochem Biophys Res Commun. 2012 Aug 10;424(4):647-50. doi:, 10.1016/j.bbrc.2012.07.024. Epub 2012 Jul 16. PMID:22814107 doi:http://dx.doi.org/10.1016/j.bbrc.2012.07.024
  3. ↑ Hatziioannou T, Perez-Caballero D, Cowan S, Bieniasz PD. Cyclophilin interactions with incoming human immunodeficiency virus type 1 capsids with opposing effects on infectivity in human cells. J Virol. 2005 Jan;79(1):176-83. PMID:15596813 doi:http://dx.doi.org/10.1128/JVI.79.1.176-183.2005
  4. ↑ Lammers M, Neumann H, Chin JW, James LC. Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization. Nat Chem Biol. 2010 May;6(5):331-7. Epub 2010 Apr 4. PMID:20364129 doi:10.1038/nchembio.342

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Cyclophilin"
Personal tools