IMR Press / FBL / Volume 23 / Issue 10 / DOI: 10.2741/4680

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.


Investigation of the structure and dynamic of calmodulin-nitric oxide synthase complexes using NMR spectroscopy

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1 Department of Chemistry, University of Waterloo, Waterloo, Ontario N2L 3G1, Canada
Front. Biosci. (Landmark Ed) 2018, 23(10), 1902–1922;
Published: 1 June 2018
(This article belongs to the Special Issue Nitric oxide: Biology and chemistry)

NMR spectroscopy allows for the determination of high resolution structures, as well as being an efficient method for studying the dynamics of protein-protein and protein-peptide complexes. 15N relaxation and H/D exchange experiments allow for the analysis of these structural dynamics at a residue specific level. Calmodulin (CaM) is a small cytosolic Ca2+ binding protein that serves as a control element for many enzymes. An important target of CaM are the nitric oxide synthase (NOS) enzymes that play a major role in a number of key physiological and pathological processes. Studies have shown CaM facilitates a conformational shift in NOS allowing for efficient electron transfer through a process thought to be highly dynamic and at least in part controlled by several possible phosphorylation sites. This review highlights recent work performed on the CaM-NOS complexes using NMR spectroscopy and shows remarkable differences in the dynamic properties of CaM-NOS complexes at physiologically relevant Ca2+ concentrations. It also shows key structural changes that affect the activity of NOS when interacting with apoCaM mutants and NOS posttranslational modifications are present.

Nitric Oxide Synthase
Protein dynamics
NMR spectroscopy
Amide exchange
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