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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.BN

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+Show Affiliations

Max Planck Research Unit for Enzymology of Protein Folding, Weinbergweg 22, 06120 Halle (Saale), Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

22287093

Citation

Linnert, Miriam, et al. "NMR Assignments of the FKBP-type PPIase Domain of the Human Aryl-hydrocarbon Receptor-interacting Protein (AIP)." Biomolecular NMR Assignments, vol. 6, no. 2, 2012, pp. 209-12.
Linnert M, Haupt K, Lin YJ, et al. NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP). Biomol NMR Assign. 2012;6(2):209-12.
Linnert, M., Haupt, K., Lin, Y. J., Kissing, S., Paschke, A. K., Fischer, G., Weiwad, M., & Lücke, C. (2012). NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP). Biomolecular NMR Assignments, 6(2), 209-12.
Linnert M, et al. NMR Assignments of the FKBP-type PPIase Domain of the Human Aryl-hydrocarbon Receptor-interacting Protein (AIP). Biomol NMR Assign. 2012;6(2):209-12. PubMed PMID: 22287093.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP). AU - Linnert,Miriam, AU - Haupt,Katja, AU - Lin,Yi-Jan, AU - Kissing,Sandra, AU - Paschke,Anne-Katrin, AU - Fischer,Gunter, AU - Weiwad,Matthias, AU - Lücke,Christian, PY - 2011/11/23/received PY - 2012/01/17/accepted PY - 2012/1/31/entrez PY - 2012/1/31/pubmed PY - 2013/2/1/medline SP - 209 EP - 12 JF - Biomolecular NMR assignments JO - Biomol NMR Assign VL - 6 IS - 2 N2 - 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. SN - 1874-270X UR - https://www.unboundmedicine.com/medline/citation/22287093/NMR_assignments_of_the_FKBP_type_PPIase_domain_of_the_human_aryl_hydrocarbon_receptor_interacting_protein__AIP__ L2 - https://dx.doi.org/10.1007/s12104-012-9359-0 DB - PRIME DP - Unbound Medicine ER -