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Related Concept Videos

Phosphorylation01:02

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...

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Solid Phase Synthesis of a Functionalized Bis-Peptide Using "Safety Catch" Methodology
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Pin1 WW Domain Ligand Library Synthesized with an Easy Solid-Phase Phosphorylating Reagent.

Xingguo R Chen1, Ana Y Mercedes-Camacho1, Kimberly A Wilson2

  • 1Department of Chemistry, Virginia Tech, Blacksburg, Virginia 24061, United States.

Biochemistry
|October 8, 2024
PubMed
Summary
This summary is machine-generated.

Researchers developed a novel peptide library to identify specific ligands for the Pin1 WW domain, a key enzyme in cell cycle regulation. This work separates Pin1

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Pin1 is a cell cycle regulatory enzyme with dual activities: catalyzing pSer/Thr-cis/trans-Pro isomerization and binding this motif via its WW domain.
  • Separating these two activities is crucial for a deeper understanding of Pin1's function.

Purpose of the Study:

  • To design and synthesize an unnatural peptide library to identify specific ligands for the Pin1 WW domain.
  • To develop a method to distinguish Pin1's binding and catalytic activities.

Main Methods:

  • A novel solid-phase phosphorylating reagent (SPPR) was synthesized for efficient preparation of a phosphoserine-containing peptide library.
  • Parallel synthesis was employed to create a 315-member unnatural peptide library (R¹CO-pSer-Pro-NHR²).
  • Screening was performed using an enzyme-linked enzyme-binding assay (ELEBA), followed by NMR chemical-shift perturbations (CSP) for validation.

Main Results:

  • A 315-member peptide library was successfully synthesized using the SPPR and parallel synthesis techniques.
  • Screening identified four high-affinity ligands specific for the Pin1 WW domain.
  • NMR CSP confirmed the specificity and allowed for the determination of dissociation constants (Kd) for the top ligands.

Conclusions:

  • The developed peptide library and screening method effectively identify specific ligands for the Pin1 WW domain.
  • These identified ligands provide valuable tools for dissecting the distinct functions of Pin1.
  • Structural modeling offers insights into the binding mode of these ligands within the Pin1 WW domain.