NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP) |
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| Authors: | Miriam Linnert Katja Haupt Yi-Jan Lin Sandra Kissing Anne-Katrin Paschke Gunter Fischer Matthias Weiwad Christian Lücke |
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| Affiliation: | 1. Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120, Halle (Saale), Germany
2. Graduate Institute of Natural Products and Center of Excellence for Environmental Medicine, Kaohsiung Medical University, Kaohsiung, 807, Taiwan
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| 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 1H, 13C and 15N chemical shift assignments for the N-terminal AIP2–166 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. |
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