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Cyclophilin

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<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>
<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>
 +
 +
== 3D Structures of Cyclophilin ==
 +
[[Cyclophilin 3D structures]]
 +
</StructureSection>
</StructureSection>
== 3D Structures of Cyclophilin ==
== 3D Structures of Cyclophilin ==
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**[[2x25]], [[2x2a]], [[3k0m]], [[3k0n]], [[1w8l]], [[1w8m]], [[1w8v]], [[1rmh]], [[2cpl]], [[5kv7]], [[5kv6]], [[5kv5]], [[5kv4]], [[5kv3]], [[5kv2]], [[5kv1]], [[5kv0]], [[5kuz]], [[5kuw]], [[5kuv]], [[5kuu]], [[5kus]], [[5kur]], [[5kuq]], [[5kuo]], [[5kun]], [[4kul]], [[5f66]], [[4yup]], [[4yuo]], [[4yun]], [[4yum]], [[4yul]], [[4yuk]], [[4yuj]], [[4yui]], [[4yuh]], [[4yug]], [[2n0t]], [[5kul]] – hCyp-A – human<br />
**[[2x25]], [[2x2a]], [[3k0m]], [[3k0n]], [[1w8l]], [[1w8m]], [[1w8v]], [[1rmh]], [[2cpl]], [[5kv7]], [[5kv6]], [[5kv5]], [[5kv4]], [[5kv3]], [[5kv2]], [[5kv1]], [[5kv0]], [[5kuz]], [[5kuw]], [[5kuv]], [[5kuu]], [[5kus]], [[5kur]], [[5kuq]], [[5kuo]], [[5kun]], [[4kul]], [[5f66]], [[4yup]], [[4yuo]], [[4yun]], [[4yum]], [[4yul]], [[4yuk]], [[4yuj]], [[4yui]], [[4yuh]], [[4yug]], [[2n0t]], [[5kul]] – hCyp-A – human<br />
**[[1oca]], [[2mzu]] – hCyp-A - NMR<br />
**[[1oca]], [[2mzu]] – hCyp-A - NMR<br />
-
**[[3k0o]], [[3k0p]], [[3k0q]], [[3k0r]], [[2alf]] – hCyp-A (mutant)<br />
+
**[[3k0o]], [[3k0p]], [[3k0q]], [[3k0r]], [[2alf]] ,[[6bta]], [[5wc7]] – hCyp-A (mutant)<br />
**[[4dgd]] - RmCyp-A (mutant) – Rhesus macaque <br />
**[[4dgd]] - RmCyp-A (mutant) – Rhesus macaque <br />
 +
**[[6fk1]] – mCyp-A – mouse<br />
**[[1ist]] – yCyp-A – yeast<br />
**[[1ist]] – yCyp-A – yeast<br />
**[[1w74]] – Cyp-A – ''Mycobacterium tuberculosis''<br />
**[[1w74]] – Cyp-A – ''Mycobacterium tuberculosis''<br />
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**[[2x2d]], [[1m9c]], [[1m9d]], [[1m9e]], [[1m9f]], [[1m9x]], [[1m9y]], [[1awq]], [[1awr]], [[1aws]], [[1awt]], [[1awu]], [[1awv]], [[1ak4]], [[1fgl]] - hCyp-A+HIV-1 N-terminal capsid domain<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 />
**[[5fjb]] - hCyp-A + HIV-1 gag protein <br />
**[[5fjb]] - hCyp-A + HIV-1 gag protein <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 />
**[[1zkf]] – hCyp-A+suc-AGPF-pNA<br />
**[[1ynd]], [[1nmk]], [[5ta4]], [[5ta2]], [[5t9z]], [[5t9w]], [[5t9u]] – hCyp-A+ sanglifehrin derivaive<br />
**[[1ynd]], [[1nmk]], [[5ta4]], [[5ta2]], [[5t9z]], [[5t9w]], [[5t9u]] – hCyp-A+ sanglifehrin derivaive<br />
-
**[[4n1s]], [[4n1r]], [[4n1q]], [[4n1p]], [[4n1o]], [[4n1n]], [[4n1m]], [[3rrd]], [[5noz]], [[5noy]], [[5nox]], [[5nou]], [[5nov]], [[5now]], [[5nor]], [[5nos]], [[5not]], [[5noq]], [[5lud]] – hCyp-A + inhibitor<br />
+
**[[4n1s]], [[4n1r]], [[4n1q]], [[4n1p]], [[4n1o]], [[4n1n]], [[4n1m]], [[3rdd]], [[5noz]], [[5noy]], [[5nox]], [[5nou]], [[5nov]], [[5now]], [[5nor]], [[5nos]], [[5not]], [[5noq]], [[5lud]], [[6gji]], [[6gjj]], [[6gjl]], [[6gjm]], [[6gjn]], [[6gjp]], [[6gjr]], [[6gjy]] – hCyp-A + inhibitor<br />
**[[2cyh]], [[3cyh]], [[4cyh]], [[5cyh]] - hCyp-A+dipeptide<br />
**[[2cyh]], [[3cyh]], [[4cyh]], [[5cyh]] - hCyp-A+dipeptide<br />
**[[1vbs]], [[1vbt]], [[2ms4]] – hCyp-A+tetrapeptide<br />
**[[1vbs]], [[1vbt]], [[2ms4]] – hCyp-A+tetrapeptide<br />
**[[4ipz]] - hCyp-A (mutant) + peptide <br />
**[[4ipz]] - hCyp-A (mutant) + peptide <br />
-
**[[1vdn]] – yCyp-A+peptidyl coumarin – yeast<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 />
 +
**[[1vdn]] – yCyp-A+peptidyl coumarin <br />
**[[1lop]] - EcCyp-A+peptidyl nitroanilide - ''Escherichia coli''<br />
**[[1lop]] - EcCyp-A+peptidyl nitroanilide - ''Escherichia coli''<br />
**[[1csa]] – EcCyp-A+ cyclosporin A – NMR<br />
**[[1csa]] – EcCyp-A+ cyclosporin A – NMR<br />
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**[[3o7t]] – NpCyp-A – ''Noniliophthora perniciosa''<br />
**[[3o7t]] – NpCyp-A – ''Noniliophthora perniciosa''<br />
**[[3pmp]] - NpCyp-A + cyclosporin A<br />
**[[3pmp]] - NpCyp-A + cyclosporin A<br />
-
**[[3rdd]] – hCyp-A + inhibitor<br />
 
**[[3t1u]] – Cyp-A + peptide – ''Azotobacter vinelandii''<br />
**[[3t1u]] – Cyp-A + peptide – ''Azotobacter vinelandii''<br />
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**[[2esl]] - hCyp-C+cyclosporin A<br />
**[[2esl]] - hCyp-C+cyclosporin A<br />
-
**[[2rmc]] - Cyp-C+cyclosporin A – mouse<br />
+
**[[2rmc]] - mCyp-C+cyclosporin A <br />
**[[1jns]], [[1jnt]] – EcCyp-C - NMR<BR />
**[[1jns]], [[1jnt]] – EcCyp-C - NMR<BR />
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**[[5a0e]] - hCyp-D (mutant) + cyclosporin A<br />
**[[5a0e]] - hCyp-D (mutant) + cyclosporin A<br />
**[[4tot]] – hCyp-D + polypeptide inhibitor<br />
**[[4tot]] – hCyp-D + polypeptide inhibitor<br />
 +
**[[5nwo]] – hCyp-D + inhibitor<br />
**[[3r49]], [[3r4g]], [[3r54]], [[3r56]], [[3r57]], [[3r59]], [[3rcf]], [[3rcg]], [[3rci]], [[3rck]], [[3rcl]], [[3rd9]], [[3rda]], [[3rdb]], [[3rdc]], [[4j58]], [[4j59]], [[4j5a]], [[4j5b]], [[4j5c]], [[4j5d]], [[5ccs]], [[5ccr]], [[5ccq]], [[5ccn]], [[5cbw]], [[5cbv]], [[5cbu]], [[5cbt]], [[4zsc]], [[4xnc]], [[4j5e]] – hCyp-D (mutant) + inhibitor<br />
**[[3r49]], [[3r4g]], [[3r54]], [[3r56]], [[3r57]], [[3r59]], [[3rcf]], [[3rcg]], [[3rci]], [[3rck]], [[3rcl]], [[3rd9]], [[3rda]], [[3rdb]], [[3rdc]], [[4j58]], [[4j59]], [[4j5a]], [[4j5b]], [[4j5c]], [[4j5d]], [[5ccs]], [[5ccr]], [[5ccq]], [[5ccn]], [[5cbw]], [[5cbv]], [[5cbu]], [[5cbt]], [[4zsc]], [[4xnc]], [[4j5e]] – hCyp-D (mutant) + inhibitor<br />
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**[[2r99]], [[3uch]] - hCyp-E ABH-like domain<br />
**[[2r99]], [[3uch]] - hCyp-E ABH-like domain<br />
**[[2cqb]] – hCyp-E RNA recognition motif<br />
**[[2cqb]] – hCyp-E RNA recognition motif<br />
-
**[[2ck1]], [[2cmt]] – Cyp-E – ''Schistosoma mansoni''<br />
 
**[[2kyx]] – hCyp-E RRM domain – NMR<br />
**[[2kyx]] – hCyp-E RRM domain – NMR<br />
**[[3lpy]], [[3mdf]] - hCyp-E RRM domain<br />
**[[3lpy]], [[3mdf]] - hCyp-E RRM domain<br />
 +
**[[2ck1]], [[2cmt]] – Cyp-E – ''Schistosoma mansoni''<br />
* Cyclophilin-G
* Cyclophilin-G
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* Cyclophilin
* Cyclophilin
 +
**[[1qoi]] – hCyp SNUCYP-20<br />
**[[3bo7]] - TgCyp+cyclosporin A - ''Toxoplasma gondii''<br />
**[[3bo7]] - TgCyp+cyclosporin A - ''Toxoplasma gondii''<br />
**[[2nul]] – EcCyp<br />
**[[2nul]] – EcCyp<br />
**[[1clh]] – EcCyp – NMR<br />
**[[1clh]] – EcCyp – NMR<br />
-
**[[1qoi]] – hCyp SNUCYP-20<br />
 
**[[3k2c]] – Cyp – ''Encephalitozoon cuniculi''<br />
**[[3k2c]] – Cyp – ''Encephalitozoon cuniculi''<br />
**[[3eov]] - LdCyp+cyclosporin A – ''Leishmania donovani''<br />
**[[3eov]] - LdCyp+cyclosporin A – ''Leishmania donovani''<br />
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**[[2ke0]], [[3s6m]] – BpCyp – NMR<br />
**[[2ke0]], [[3s6m]] – BpCyp – NMR<br />
**[[4dz2]], [[4dz3]] – BpPin1 (mutant) + FK506<BR />
**[[4dz2]], [[4dz3]] – BpPin1 (mutant) + FK506<BR />
 +
**[[2wlw]] - Cyp – macaca mulata <br />
 +
**[[2mc9]] - Cyp – rosy periwinkle <br />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 09:56, 22 May 2019

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

3D Structures of Cyclophilin

Updated on 22-May-2019

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

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Michal Harel, Alexander Berchansky

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