title: ¹H, ¹³C and ¹⁵N resonance assignments of human parvulin 17.
abstract: A 25-residue elongation at the N-terminus endows parvulin 17 (Par17) with altered functional properties compared to parvulin 14 (Par14), such as an enhanced influence on microtubule assembly. Therefore the three-dimensional structure of this N-terminal elongation is of particular interest. Here, we report the nearly complete (1)H, (13)C and (15)N chemical shift assignments of Par17. Subsequent chemical shift index analysis indicated that Par17 features a parvulin-type PPIase domain at the C-terminus, analogous to Par14, and an unstructured N-terminus encompassing the first 60 residues. Hence the N-terminus of Par17 apparently adopts a functionally-relevant structure only in presence of the respective interaction partner(s).
authors.affiliation: Graduate Institute of Natural Products and Center of Excellence for Environmental Medicine, Kaohsiung Medical University, Kaohsiung 807, Taiwan.
authors.forename: Yi-Jan
authors.initials: YJ
authors.lastname: Lin
authors.forename: Andreas
authors.initials: A
authors.lastname: Schmidt
authors.forename: Noelia Inés
authors.initials: NI
authors.lastname: Burgardt
authors.forename: Alexandra
authors.initials: A
authors.lastname: Thiele
authors.forename: Matthias
authors.initials: M
authors.lastname: Weiwad
authors.forename: Christian
authors.initials: C
authors.lastname: Lücke
mesh_terms: D000595:Amino Acid Sequence; D002247:Carbon Isotopes; D006801:Humans; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry*; D011522:Protons
chemical_list: D002247:Carbon Isotopes; D000072340:NIMA-Interacting Peptidylprolyl Isomerase; D009587:Nitrogen Isotopes; D011522:Protons; C000606846:PIN1 protein, human; C000606848:PIN4 protein, human; D019696:Peptidylprolyl Isomerase