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Cyclophilin information


Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Ribbon diagram of cyclophilin A in complex with ciclosporin (yellow). From PDB: 1CWA​.
Identifiers
SymbolPro_isomerase
PfamPF00160
Pfam clanCL0475
InterProIPR002130
PROSITEPDOC00154
SCOP21cyh / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Cyclophilins (CYPs) are a family of proteins named after their ability to bind to ciclosporin (cyclosporin A), an immunosuppressant which is usually used to suppress rejection after internal organ transplants.[1] They are found in all domains of life. These proteins have peptidyl prolyl isomerase activity, which catalyzes the isomerization of peptide bonds from trans form to cis form at proline residues and facilitates protein folding.

Cyclophilin A is a cytosolic and highly abundant protein. The protein belongs to a family of isozymes, including cyclophilins B and C, and natural killer cell cyclophilin-related protein.[2][3][4] Major isoforms have been found within single cells, including inside the Endoplasmic reticulum, and some are even secreted.

  1. ^ Stamnes MA, Rutherford SL, Zuker CS (September 1992). "Cyclophilins: a new family of proteins involved in intracellular folding". Trends Cell Biol. 2 (9): 272–6. doi:10.1016/0962-8924(92)90200-7. PMID 14731520.
  2. ^ Trandinh CC, Pao GM, Saier MH (December 1992). "Structural and evolutionary relationships among the immunophilins: two ubiquitous families of peptidyl-prolyl cis-trans isomerases". FASEB J. 6 (15): 3410–20. doi:10.1096/fasebj.6.15.1464374. PMID 1464374. S2CID 30435500.
  3. ^ Galat A (September 1993). "Peptidylproline cis-trans-isomerases: immunophilins". Eur. J. Biochem. 216 (3): 689–707. doi:10.1111/j.1432-1033.1993.tb18189.x. PMID 8404888.
  4. ^ Hacker J, Fischer G (November 1993). "Immunophilins: structure-function relationship and possible role in microbial pathogenicity". Mol. Microbiol. 10 (3): 445–56. doi:10.1111/j.1365-2958.1993.tb00917.x. PMID 7526121. S2CID 13160331.

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Cyclophilin

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Cyclophilins (CYPs) are a family of proteins named after their ability to bind to ciclosporin (cyclosporin A), an immunosuppressant which is usually used...

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Peptidylprolyl isomerase A

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Peptidylprolyl isomerase A (PPIA), also known as cyclophilin A (CypA) or rotamase A is an enzyme that in humans is encoded by the PPIA gene on chromosome...

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FKBP

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proteins that have prolyl isomerase activity and are related to the cyclophilins in function, though not in amino acid sequence. FKBPs have been identified...

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PPIB

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as in a few archaebacteria, and thus are highly conserved. Like other cyclophilins, PPIB forms a β-barrel structure with a hydrophobic core. This β-barrel...

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Peptidylprolyl isomerase D

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Peptidylprolyl isomerase D (cyclophilin D), also known as PPID, is an enzyme which in humans is encoded by the PPID gene on chromosome 4. As a member...

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Chordate

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identified two conserved signature indels (CSIs) in their proteins: cyclophilin-like protein and inner mitochondrial membrane protease ATP23, which are...

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Ciclosporin

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the function of lymphocytes. It does this by forming a complex with cyclophilin to block the phosphatase activity of calcineurin, which in turn decreases...

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PPIF

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gene. It has also been referred to as, but should not be confused with, cyclophilin D (CypD), which is encoded by the PPID gene. As a member of the peptidyl-prolyl...

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Rencofilstat

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Rencofilstat (CRV431) is a pan-cyclophilin inhibitor and analog of cyclosporine A developed for nonalcoholic steatohepatitis and hepatocellular carcinoma...

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Sanglifehrin

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Sanglifehrin A is a polyketide natural product found to potently inhibit cyclophilins and have immunosuppressive activity. Isolation and characterisation of...

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Alisporivir

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UNIL-025) is a cyclophilin inhibitor. Its structure is reminiscent of, and synthesized from ciclosporin.[citation needed] It inhibits cyclophilin A. Alisporivir...

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Calcineurin

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HUMAN CALCINEURIN HETERODIMER 1m63: Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug...

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CYP

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alpha-3 country code for Cyprus CYP, ISO 4217 code for the Cypriot pound Cyclophilin Cytochrome P450, isoenzyme Cypripedium, orchid genus This disambiguation...

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Becker muscular dystrophy

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The investigational drug Debio-025 is a known inhibitor of the protein cyclophilin D, which regulates the swelling of mitochondria in response to cellular...

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Prolyl isomerase

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relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl...

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Reperfusion injury

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Cyclosporin has been confirmed in studies to inhibit the actions of cyclophilin D, a protein which is induced by excessive intracellular calcium flow...

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Immunosuppressive drug

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protein cyclophilin (an immunophilin) of immunocompetent lymphocytes, especially T-lymphocytes. This complex of ciclosporin and cyclophilin inhibits...

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Hepatitis C

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C. These include vaccines to treat hepatitis, immunomodulators, and cyclophilin inhibitors, among others. These potential new treatments have come about...

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PPIC

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conditions, such as ischemic reperfusion injury, AIDS, and cancer. Like other cyclophilins, PPIC forms a β-barrel structure with a hydrophobic core. This β-barrel...

Word Count : 1387

NIM811

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cyclosporin, it is a four-substituted cyclosporine analogue that binds to cyclophilin, however this binary complex cannot bind to calcineurin, and therefore...

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PPIH

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of Medicine. Horowitz DS, Kobayashi R, Krainer AR (Dec 1997). "A new cyclophilin and the human homologues of yeast Prp3 and Prp4 form a complex associated...

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Protein family

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The human cyclophilin family, as represented by the structures of the isomerase domains of some of its members...

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Telitacicept

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combines a recombinant transmembrane activator and calcium modulator and cyclophilin ligand interactor (TACI) and a fragment of human immunoglobulin G (IgG)...

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Abdominal aortic aneurysm

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complications. By eliminating the gene for a signaling protein called cyclophilin A (CypA) from a strain of mice, researchers were able to provide complete...

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Tacrolimus

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Weissman I, Schreiber SL (August 1991). "Calcineurin is a common target of cyclophilin-cyclosporin A and FKBP-FK506 complexes". Cell. 66 (4): 807–815. doi:10...

Word Count : 4357

Necroptosis

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which represses the mitochondrial permeability transition effector Cyclophilin D, improves tissue survival primarily by inhibiting necrotic cell death...

Word Count : 1667

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