NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP)

Miriam Linnert; Katja Haupt; Yi-Jan Lin; Sandra Kissing; Anne-Katrin Paschke; Gunter Fischer; Matthias Weiwad; Christian Lücke

doi:10.1007/s12104-012-9359-0

NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP)

Biomol NMR Assign. 2012 Oct;6(2):209-12. doi: 10.1007/s12104-012-9359-0.

Authors

Miriam Linnert¹, Katja Haupt, Yi-Jan Lin, Sandra Kissing, Anne-Katrin Paschke, Gunter Fischer, Matthias Weiwad, Christian Lücke

Affiliation

¹ Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany.

PMID: 22287093
DOI: 10.1007/s12104-012-9359-0

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Humans
Intracellular Signaling Peptides and Proteins / chemistry*
Nuclear Magnetic Resonance, Biomolecular*
Peptidylprolyl Isomerase / chemistry*
Protein Structure, Secondary
Protein Structure, Tertiary
Tacrolimus Binding Proteins / chemistry*

Substances

Intracellular Signaling Peptides and Proteins
aryl hydrocarbon receptor-interacting protein
Tacrolimus Binding Proteins
Peptidylprolyl Isomerase