Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery

Born, Alexandra; Nichols, Parker J.; Henen, Morkos A.; Chi, Celestine N.; Strotz, Dean; Bayer, Peter; Tate, Shin-Ichi; Peng, Jeffrey W.; Vögeli, Beat

doi:10.1007/s12104-018-9857-9

Article
Published: 23 October 2018

Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery

Alexandra Born¹,
Parker J. Nichols¹,
Morkos A. Henen^1,2,
Celestine N. Chi³,
Dean Strotz⁴,
Peter Bayer⁵,
Shin-Ichi Tate⁶,
Jeffrey W. Peng⁷ &
Beat Vögeli ORCID: orcid.org/0000-0003-1176-3137^1,8

Biomolecular NMR Assignments volume 13, pages 85–89 (2019)Cite this article

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Abstract

Pin1 is a human peptidyl-prolyl cis–trans isomerase important for the regulation of phosphoproteins that are implicated in many diseases including cancer and Alzheimer’s. Further biophysical study of Pin1 will elucidate the importance of the two-domain system to regulate its own activity. Here, we report near-complete backbone and side-chain ¹H, ¹³C and ¹⁵N NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics.

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Acknowledgements

We would like to thank Dr. David Jones at University of Colorado for helping set up initial experiments. This work was supported by a start-up package from the University of Colorado at Denver to B.V.

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Affiliations

Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA
Alexandra Born, Parker J. Nichols, Morkos A. Henen & Beat Vögeli
Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt
Morkos A. Henen
Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, 75123, Uppsala, Sweden
Celestine N. Chi
Laboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zurich, Switzerland
Dean Strotz
Strukturelle und Medizinische Biochemie, Universität Duisburg-Essen, Universitätsstrasse 2-5, 45117, Essen, Germany
Peter Bayer
Department of Mathematical and Life Sciences, Hiroshima University, Hiroshima, Japan
Shin-Ichi Tate
Department of Chemistry and Biochemistry & Department of Physics, University of Notre Dame, Notre Dame, IN, 46556, USA
Jeffrey W. Peng
Department of Biochemistry and Molecular Genetics, University of Colorado Denver, Research Center 1 South, Room 9103, 12801 East 17th Avenue, Aurora, CO, 80045, USA
Beat Vögeli

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Alexandra Born
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Parker J. Nichols
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Morkos A. Henen
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Celestine N. Chi
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Dean Strotz
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Peter Bayer
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Shin-Ichi Tate
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Jeffrey W. Peng
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Beat Vögeli
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Correspondence to Beat Vögeli.

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Born, A., Nichols, P.J., Henen, M.A. et al. Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery. Biomol NMR Assign 13, 85–89 (2019). https://doi.org/10.1007/s12104-018-9857-9

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Received: 14 September 2018
Accepted: 19 October 2018
Published: 23 October 2018
Issue Date: 01 April 2019
DOI: https://doi.org/10.1007/s12104-018-9857-9

Keywords

Pin1
Prolyl isomerase
NMR
Chemical shift assignments
Allostery