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Literature DB >> 30353504

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^8,9.

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.

Entities: Chemical

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

Mesh：

Substances：

Year: 2018 PMID： 30353504 PMCID： PMC9205186 DOI： 10.1007/s12104-018-9857-9

Source DB: PubMed Journal: Biomol NMR Assign ISSN： 1874-270X Impact factor: 0.731

25 in total

1. Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

Authors: Doris M Jacobs; Krishna Saxena; Martin Vogtherr; Pau Bernado; Miquel Pons; Klaus M Fiebig
Journal: J Biol Chem Date: 2003-04-09 Impact factor: 5.157

Review 2. Pin1 in Alzheimer's disease.

Authors: D Allan Butterfield; Hafiz Mohmmad Abdul; Wycliffe Opii; Shelley F Newman; Gururaj Joshi; Mubeen Ahmad Ansari; Rukhsana Sultana
Journal: J Neurochem Date: 2006-09 Impact factor: 5.372

3. Substrate recognition reduces side-chain flexibility for conserved hydrophobic residues in human Pin1.

Authors: Andrew T Namanja; Tao Peng; John S Zintsmaster; Andrew C Elson; Maria G Shakour; Jeffrey W Peng
Journal: Structure Date: 2007-03 Impact factor: 5.006

4. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.

Authors: R Ranganathan; K P Lu; T Hunter; J P Noel
Journal: Cell Date: 1997-06-13 Impact factor: 41.582

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

1. Peptide binding induces large scale changes in inter-domain mobility in human Pin1.

Review 2. Pin1 in Alzheimer's disease.

3. Substrate recognition reduces side-chain flexibility for conserved hydrophobic residues in human Pin1.

4. Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.

5. Propagated Perturbations from a Peripheral Mutation Show Interactions Supporting WW Domain Thermostability.

6. NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

7. The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins.

8. 1H, 13C and 15N backbone resonance assignment of the peptidyl-prolyl cis-trans isomerase Pin1.

9. Investigating Dynamic Interdomain Allostery in Pin1.

10. Efficient Stereospecific H^β2/3 NMR Assignment Strategy for Mid-Size Proteins.

1. Reconstruction of Coupled Intra- and Interdomain Protein Motion from Nuclear and Electron Magnetic Resonance.

2. Reducing the measurement time of exact NOEs by non-uniform sampling.

3. Ligand-specific conformational change drives interdomain allostery in Pin1.

4. New Benzimidazoles Targeting Breast Cancer: Synthesis, Pin1 Inhibition, 2D NMR Binding, and Computational Studies.