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

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

doi:10.1007/s12104-018-9857-9

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

Biomol NMR Assign. 2019 Apr;13(1):85-89. doi: 10.1007/s12104-018-9857-9. Epub 2018 Oct 23.

Authors

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^{8

9}

Affiliations

¹ Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA.
² Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt.
³ Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, 75123, Uppsala, Sweden.
⁴ Laboratory of Physical Chemistry, ETH Zürich, ETH-Hönggerberg, Zurich, Switzerland.
⁵ Strukturelle und Medizinische Biochemie, Universität Duisburg-Essen, Universitätsstrasse 2-5, 45117, Essen, Germany.
⁶ Department of Mathematical and Life Sciences, Hiroshima University, Hiroshima, Japan.
⁷ Department of Chemistry and Biochemistry & Department of Physics, University of Notre Dame, Notre Dame, IN, 46556, USA.
⁸ Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA. beat.vogeli@ucdenver.edu.
⁹ 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.vogeli@ucdenver.edu.

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.

Keywords: Allostery; Chemical shift assignments; NMR; Pin1; Prolyl isomerase.

Publication types

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

MeSH terms

Allosteric Regulation
Apoproteins / chemistry*
Humans
NIMA-Interacting Peptidylprolyl Isomerase / chemistry*
Nuclear Magnetic Resonance, Biomolecular*
Phosphoproteins / chemistry*
Protein Domains

Substances

Apoproteins
NIMA-Interacting Peptidylprolyl Isomerase
Phosphoproteins
PIN1 protein, human

Grants and funding

P30 CA046934/CA/NCI NIH HHS/United States