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

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.

• Authors: Alexandra Born, Parker J Nichols, Morkos A Henen, Celestine N Chi, Dean Strotz, Peter Bayer, Shin-Ichi Tate, Jeffrey W Peng, Beat Vögeli
• Journal: Biomolecular NMR assignments (Biomol NMR Assign) Vol. 13 Issue 1 Pg. 85-89 (04 2019) ISSN: 1874-270X [Electronic] Netherlands
• PMID: 30353504 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Apoproteins
• NIMA-Interacting Peptidylprolyl Isomerase
• Phosphoproteins
• PIN1 protein, human

Topics

• Allosteric Regulation
• Apoproteins (chemistry)
• Humans
• NIMA-Interacting Peptidylprolyl Isomerase (chemistry)
• Nuclear Magnetic Resonance, Biomolecular
• Phosphoproteins (chemistry)
• Protein Domains