Open AccessBackbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery
Author(s) -
Alexandra Born,
Parker J. Nichols,
Morkos A. Henen,
N. Celestine,
Dean Strotz,
Peter Bayer,
Shinichi Tate,
Jeffrey W. Peng,
Beat Vögeli
Publication year - 2018
Publication title -
biomolecular nmr assignments
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.359
H-Index - 16
eISSN - 1874-2718
pISSN - 1874-270X
DOI - 10.1007/s12104-018-9857-9
Subject(s) - pin1 , allosteric regulation , phosphoprotein , side chain , regulator , chemistry , biophysics , isomerase , stereochemistry , biochemistry , biology , phosphorylation , gene , polymer , organic chemistry , enzyme
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 1 H, 13 C and 15 N NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics.