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When proton-coupled carbon-13 spectra are simplified by a broadband proton decoupling technique, structural information about the coupled protons is lost. Distortionless enhancement by polarization transfer (DEPT) is a technique that provides information on the number of hydrogens attached to each carbon in a molecule. While the DEPT experiment utilizes complex pulse sequences, the pulse delay and flip angle are specifically manipulated. The resulting signals have different phases depending on...
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Backbone resonance assignments of CPEB3 [1-120], CPEB3 [186-315], and CPEB3 [400-459].

Yujin Lee1, Harunobu Saito1, Masatomo So1

  • 1Graduate school of agriculture, Kyoto University, Kyoto, Japan.

Biomolecular NMR Assignments
|May 29, 2026
PubMed
Summary

Cytoplasmic polyadenylation element-binding protein 3 (CPEB3) is crucial for memory. This study reveals structural insights into its disordered N-terminal region, identifying partial helical structures that may govern its function.

Keywords:
CPEB3IDRLong-term memoryProtein aggregation

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Cytoplasmic polyadenylation element-binding protein 3 (CPEB3) is vital for long-term memory formation.
  • Its N-terminal intrinsically disordered region regulates mRNA translation via phase separation and fibril formation.
  • The molecular mechanisms underlying CPEB3's regulation are not well understood.

Purpose of the Study:

  • To investigate the structural properties of the intrinsically disordered N-terminal region of CPEB3.
  • To provide backbone resonance assignments for key segments of CPEB3's disordered region.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine backbone resonance assignments.
  • Three specific segments of the CPEB3 N-terminal region (residues 1-120, 186-315, and 400-459) were analyzed.

Main Results:

  • The analyzed segments of CPEB3 were predominantly disordered, consistent with predictions.
  • Short regions exhibiting partial helical propensity were identified within the 1-120 segment (residues 3-7) and the 186-315 segment (residues 226-239).

Conclusions:

  • These findings provide initial structural data for the intrinsically disordered region of CPEB3.
  • The identified partial helical structures may play a role in CPEB3's aggregation and regulatory functions in memory formation.