Sandbox Reserved 1135

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This Sandbox is Reserved from 15/12/2015, through 15/06/2016 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1120 through Sandbox Reserved 1159.
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Contents

Introduction

Endothelial Nitric Oxide Synthase (eNOS)[1] is a major actor in the regulation of cardiovascular processes, since it induces the production of Nitric Oxide (NO) in vascular endothelial cells. NO is involved in several processes such as vessel vasodilatation, vascular smooth muscle cell proliferation, angiogenesis. The activity of eNOS is related to intracellular calcium concentration and its activation requires the calcium binding protein, CalModulin (CaM).

The structure of CaM protein bound to the CaM binding domain of eNOS has been obtained thanks to a solution NMR[2], a nuclear magnetic resonance that enables the determination of structures but also interactions between molecules.

Structure and function

Production of NO

Structure of CaM

Calmodulin is a 148-amino-acid peptide containing two symmetrical globular calcium domains connected by a flexible central linker region that is a 28-amino-acid-long alpha helix. CaM has 4 EF hand motifs (two at each globular calcium binding domain) highly conserved among calcium binding proteins. EF hand motif is suitable for the binding of one calcium ion since an electronegative environment is established (12-74 & 85-147).

Structure of eNOS

Interaction between CaM and the CaM binding domain peptide of eNOS

The 3D structure[3] shown here represents the interaction between the and the .

Disease

As NO has a really important role in cardiovascular processes, a malfunction in the production of NO can contribute to diseases such as atherosclerosis, hypertension.

References

  1. ↑ eNOS signaling[1]
  2. ↑ Solution NMR, Instruct Interacting Biology. [2]
  3. ↑ Structure from PDB[3]
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