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Long-range coupling between separate docking sites in interleukin-1beta.

David K Heidary1, Melinda Roy, Gaston O Daumy

  • 1Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, CA 92093-0359, USA.

Journal of Molecular Biology
|October 12, 2005
PubMed
Summary
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A single histidine residue in interleukin-1beta (IL-1beta) significantly impacts receptor binding and protein stability. Mutations revealed how this residue influences interactions at distant sites, affecting IL-1beta function.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Interleukin-1beta (IL-1beta) is a key cytokine mediating inflammatory responses.
  • IL-1beta binds to the interleukin type I receptor via two distinct docking surfaces, A and B.
  • Specific residues at the receptor/ligand interface are crucial for binding affinity and biological activity.

Purpose of the Study:

  • To investigate the functional role of histidine 30 (His30) in IL-1beta's site A.
  • To determine how mutations at His30 affect IL-1beta protein stability and receptor binding.
  • To elucidate the mechanism of allosteric communication between docking sites A and B in IL-1beta.

Main Methods:

  • Site-directed mutagenesis was used to create four IL-1beta mutants (H30A, H30D, H30F, H30R).

Related Experiment Videos

  • Protein stability was assessed through methods like native solvent exchange.
  • Receptor binding was evaluated using a single-chain antibody specific for site B, and structural changes were probed using dihedral scalar coupling constants.

    • Main Results:

    • The H30D mutation, introducing charge repulsion, destabilized the protein but had minimal impact on receptor binding.
    • Mutations H30F and H30R, enhancing hydrophobic or electrostatic interactions, impaired receptor binding significantly with little effect on stability.
    • All mutations demonstrated communication from site A to site B, evidenced by altered antibody binding and changes in backbone angles near site B.

    Conclusions:

    • A single residue, His30 in IL-1beta site A, plays a critical role in modulating protein stability and receptor binding affinity.
    • Perturbations at His30 can induce long-range effects, influencing the conformation and function of the distant site B.
    • The findings highlight the intricate network of interactions governing cytokine-receptor complex formation and allosteric regulation.