Chemical shift perturbations induced by residue specific mutations of CaM interacting with NOS peptides
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Date
2015-10-01
Authors
Piazza, Michael
Guillemette, J. Guy
Dieckmann, Thorsten
Journal Title
Journal ISSN
Volume Title
Publisher
Springer
Abstract
The regulation of nitric oxide synthase (NOS) by calmodulin (CaM) plays a major role in a number of key physiological and pathological processes. A detailed molecular level picture of how this regulation is achieved is critical for drug development and for our understanding of protein regulation in general. CaM is a small acidic calcium binding protein and is required to fully activate NOS. The exact mechanism of how CaM activates NOS is not fully understood at this time. Studies have shown CaM to act like a switch that causes a conformational change in NOS to allow for the electron transfer between the reductase and oxygenase domains through a process that is thought to be highly dynamic. The interaction of CaM with NOS is modified by a number of post-translation modifications including phosphorylation. Here we present backbone and sidechain 1H, 15N NMR assignments of modified CaM interacting with NOS peptides which provides the basis for a detailed study of CaM–NOS interaction dynamics using 15N relaxation methods.
Description
The final publication is available at Springer via http://dx.doi.org/10.1007/s12104-015-9596-0
Keywords
Calmodulin, Nitric oxide synthase, NMR spectroscopy, Resonance assignment