Cyclophilin

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<StructureSection load='2x25' size='350' side='right' caption='Human Cyclophilin-A with acetyllysine (PDB entry [[2x25]])' scene=''>
<StructureSection load='2x25' size='350' side='right' caption='Human Cyclophilin-A with acetyllysine (PDB entry [[2x25]])' scene=''>
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== Function ==
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[[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>
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== Relevance ==
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[[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>
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Cyc
</StructureSection>
</StructureSection>
== 3D Structures of Cyclophilin ==
== 3D Structures of Cyclophilin ==

Revision as of 08:21, 17 December 2015

Human Cyclophilin-A with acetyllysine (PDB entry 2x25)

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3D Structures of Cyclophilin

Updated on 17-December-2015

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

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Michal Harel, Alexander Berchansky

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