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Activity of Tumor Necrosis Factor α Is Modulated by Dynamic Conformational Rearrangements.

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Tumor necrosis factor α (TNFα) inactivation was studied using NMR. Perturbing the TNFα interface increases its dynamics, offering new strategies for targeting inflammatory diseases.

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Area of Science:

  • Biochemistry
  • Immunology
  • Structural Biology

Background:

  • Tumor necrosis factor α (TNFα) is a critical cytokine regulating immune responses.
  • Deregulated TNFα activity is implicated in major chronic inflammatory diseases.
  • Inactivating TNFα by disrupting its protein-protein interface is a therapeutic strategy, but its mechanism is unclear.

Purpose of the Study:

  • To elucidate the atomic-resolution mechanism of TNFα inactivation.
  • To investigate the solution structure and dynamics of active and inactive TNFα.
  • To understand how interface perturbation affects TNFα conformation and dynamics.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy to probe solution structure and dynamics.
  • Site-directed mutagenesis of residues at the trimerization interface.
  • Targeting the TNFα interface with a low molecular weight inhibitor.

Main Results:

  • TNFα exhibits motions across various timescales.
  • Perturbation of the TNFα interface did not alter its overall structure or trimeric state.
  • Inactivation led to increased conformational dynamics from the interface to receptor-binding regions.

Conclusions:

  • TNFα inactivation involves increased conformational dynamics rather than complete structural collapse.
  • These findings provide mechanistic insights into TNFα inactivation.
  • The study lays the groundwork for developing novel strategies to target TNFα activity in inflammatory diseases.