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Capturing cyclic nucleotides in action: snapshots from crystallographic studies.

Holger Rehmann1, Alfred Wittinghofer, Johannes L Bos

  • 1Department of Physiological Chemistry and Centre for Biomedical Genetics, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands. h.rehmann@UMCutrecht.nl

Nature Reviews. Molecular Cell Biology
|December 22, 2006
PubMed
Summary

Cyclic nucleotides like cAMP regulate cellular processes by activating specific proteins. Recent structural studies reveal a general mechanism for how these molecules control protein function.

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Area of Science:

  • Molecular Biology
  • Cellular Signaling

Background:

  • Cyclic adenosine monophosphate (cAMP) was discovered 50 years ago as a crucial second messenger in hormone action.
  • cAMP and cyclic guanosine monophosphate (cGMP) regulate numerous cellular functions.
  • Cyclic nucleotides activate effectors including protein kinase A, protein kinase G, cyclic-nucleotide-regulated ion channels, and Epac.

Purpose of the Study:

  • To elucidate the general structural mechanism by which cyclic nucleotides regulate their target proteins.
  • To integrate recent structural findings into a cohesive understanding of cyclic nucleotide signaling.

Main Methods:

  • Structural biology analyses
  • Biochemical assays
  • Comparative protein structure analysis

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Last Updated: Jul 10, 2026

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Main Results:

  • Identification of conserved structural motifs involved in cyclic nucleotide binding.
  • Elucidation of conformational changes induced in effector proteins upon cyclic nucleotide binding.
  • Proposal of a unified structural model for cyclic nucleotide-protein interactions.

Conclusions:

  • Cyclic nucleotides regulate a diverse set of proteins through conserved structural mechanisms.
  • Understanding these mechanisms provides insights into signal transduction pathways.
  • Structural insights pave the way for targeted modulation of cyclic nucleotide signaling pathways.