Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding

The peptidyl-prolyl cis/trans isomerase hPin1 is a phosphorylation-dependent regulatory enzyme whose substrates are proteins involved in regulation of cell cycle, transcription, Alzheimer's disease, and cancer pathogenesis. We have determined the solution structure of the two domain protein hPi...

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Veröffentlicht in:	The Journal of biological chemistry 2003-07, Vol.278 (28), p.26183-26193
Hauptverfasser:	Bayer, Elena, Goettsch, Sandra, Mueller, Jonathan W, Griewel, Bernhard, Guiberman, Elena, Mayr, Lorenz M, Bayer, Peter
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Binding Sites Catalytic Domain Crystallography, X-Ray Dose-Response Relationship, Drug Humans Hydrogen-Ion Concentration Ions - pharmacology Magnetic Resonance Spectroscopy Microscopy, Fluorescence Mitosis Models, Molecular Molecular Sequence Data NIMA-Interacting Peptidylprolyl Isomerase Peptidylprolyl Isomerase - chemistry Peptidylprolyl Isomerase - metabolism Plasmids - metabolism Protein Binding Protein Conformation Protein Structure, Tertiary Protons Spectrometry, Fluorescence Substrate Specificity Temperature Time Factors Ultraviolet Rays
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Zusammenfassung:	The peptidyl-prolyl cis/trans isomerase hPin1 is a phosphorylation-dependent regulatory enzyme whose substrates are proteins involved in regulation of cell cycle, transcription, Alzheimer's disease, and cancer pathogenesis. We have determined the solution structure of the two domain protein hPin1-(1-163) and its separately expressed PPIase domain (50-163) (hPin1PPIase) with an root mean square deviation of
ISSN:	0021-9258
DOI:	10.1074/jbc.M300721200