Disease relevance of PPIE

• Co-amplification of a novel cyclophilin-like gene (PPIE) with L-myc in small cell lung cancer cell lines [1].
• We isolated the hCyP33 gene from the human hematopoietic stem/progenitor cells and expressed it in Escherichia coli, and determined the crystal structure of the C domain of hCyP33 at 1.88 A resolution [2].

High impact information on PPIE

• Histone deacetylase 1 interacts with the MLL repression domain, partially mediating its activity; binding of Cyp33 to the adjacent MLL-PHD domain potentiates this binding [3].
• This gene, tentatively named PPIE (peptidyl-prolyl cis-trans isomerase E), has 83% amino acid identity with the central conserved region of cyclophilin A, is evolutionarily conserved by Southern blot, and exhibits differential tissue expression with highest levels found in muscle and brain [1].
• The prognostic and functional consequences of PPIE gene amplification in SCLC can now be determined [1].
• Here we describe a novel nuclear cyclophilin (hCyP33) from human T cells with an additional RNA-binding domain [4].
• A key residue of the active site is changed from Ala-103-CypA to Ser-239-hCyP33, which may affect the PPIase domain/substrates interactions [2].

Anatomical context of PPIE

• Co-amplification of PPIE was observed in seven of eleven L-myc amplified cell lines [1].

Associations of PPIE with chemical compounds

• Superposition of the structure of the C domain of hCyP33 with the structure of CypA suggests that the C domain contains PPIase active site which binds to CsA [2].

References