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PPIL1 is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases).
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molecular model for the binding mode of SKIP to PPIL1 which emphasizes the versatility of cyclophilin (Montrer PPIA Anticorps)-type PPIases to engage in additional interactions with other proteins apart from active site contacts despite their limited surface area.
The large disordered region in SKIP provides an interaction platform. Its disorder-order transition, induced by PPIL1 binding, may adapt the requirement for a large structural rearrangement occurred in the activation of spliceosome
NMR protein structure of PPIL1
here the solution structure of PPIL1 determined by NMR spectroscopy
This gene is a member of the cyclophilin family of peptidylprolyl isomerases (PPIases). The cyclophilins are a highly conserved, ubiquitous family, members of which play an important role in protein folding, immunosuppression by cyclosporin A, and infection of HIV-1 virions. Based on similarity to other PPIases, this protein could accelerate the folding of proteins and might catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
cyclophilin-related gene 1
, peptidyl-prolyl cis-trans isomerase
, peptidyl-prolyl cis-trans isomerase-like 1
, rotamase PPIL1
, peptidylprolyl isomerase (cyclophilin)-like 1
, peptidylprolyl isomerase-like 1
, peptidyl-prolyl cis-trans isomerase-like 1-like