title: NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP).
abstract: The aryl-hydrocarbon receptor-interacting protein (AIP) interacts with several protein binding partners and has been associated with pituitary tumor development. Here, we report nearly complete (1)H, (13)C and (15)N chemical shift assignments for the N-terminal AIP(2-166) segment, which has been predicted to represent a FKBP-type PPIase domain. Sequence alignment with the prototypic FKBP12, however, reveals disagreements between the AIP chemical shift index consensus and the corresponding FKBP12 secondary structure elements.
authors.affiliation: Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany.
authors.forename: Miriam
authors.initials: M
authors.lastname: Linnert
authors.forename: Katja
authors.initials: K
authors.lastname: Haupt
authors.forename: Yi-Jan
authors.initials: YJ
authors.lastname: Lin
authors.forename: Sandra
authors.initials: S
authors.lastname: Kissing
authors.forename: Anne-Katrin
authors.initials: AK
authors.lastname: Paschke
authors.forename: Gunter
authors.initials: G
authors.lastname: Fischer
authors.forename: Matthias
authors.initials: M
authors.lastname: Weiwad
authors.forename: Christian
authors.initials: C
authors.lastname: Lücke
mesh_terms: D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D019696:Peptidylprolyl Isomerase / Q000737:chemistry*; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D022021:Tacrolimus Binding Proteins / Q000737:chemistry*
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; C103265:aryl hydrocarbon receptor-interacting protein; D022021:Tacrolimus Binding Proteins; D019696:Peptidylprolyl Isomerase