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Related Experiment Videos

Structural basis for endothelial nitric oxide synthase binding to calmodulin.

Mika Aoyagi1, Andrew S Arvai, John A Tainer

  • 1Department of Molecular Biology and The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.

The EMBO Journal
|February 8, 2003
PubMed
Summary

Calmodulin (CaM) regulates nitric oxide synthase (NOS) isozymes. Crystallographic structures reveal how CaM binds to endothelial NOS (eNOS) peptides, explaining differential activation and specific interactions.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Signaling

Background:

  • Nitric oxide synthase (NOS) enzymes produce nitric oxide (NO), a crucial signaling molecule and cytotoxin.
  • Calmodulin (CaM), a calcium sensor, regulates NOS isozyme activity, but the mechanisms remain unclear.
  • Understanding differential CaM-NOS interactions is key to deciphering NO production control.

Purpose of the Study:

  • To elucidate the structural basis for differential activation of NOS isozymes by CaM.
  • To determine the conformations and interactions between CaM and an endothelial NOS (eNOS) peptide.
  • To explain isozyme-specific differences in CaM binding and NOS activation.

Main Methods:

  • Crystallographic analysis of Ca(2+)-loaded CaM bound to a 20-residue eNOS CaM-binding peptide.

Related Experiment Videos

  • Detailed examination of intermolecular interactions and conformational changes.

    • Main Results:

    • The eNOS peptide adopts an alpha-helical structure and binds antiparallel to CaM via hydrophobic interactions.
    • Specific interactions involve the CaM central linker, crucial for NOS activation.
    • CaM C-terminus interactions explain eNOS deactivation by phosphorylation and Ca(2+)-independent activation of inducible NOS.

    Conclusions:

    • The determined binding mode expands the understanding of CaM-mediated activation mechanisms.
    • Structural insights explain eNOS deactivation by Thr495 phosphorylation.
    • Specific hydrophobic residues are implicated in the Ca(2+)-independent activation of inducible NOS.