KOPS - The Institutional Repository of the University of Konstanz

The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2

The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2

Cite This

Files in this item

Files Size Format View

There are no files associated with this item.

THEISGEN, Stephan, Lars THOMAS, Thomas SCHRÖDER, Christian LANGE, Michael KOVERMANN, Jochen BALBACH, Daniel HUSTER, 2011. The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2. In: European Biophysics Journal : EBJ. 40(4), pp. 565-576. ISSN 0175-7571. eISSN 1432-1017. Available under: doi: 10.1007/s00249-011-0680-9

@article{Theisgen2011-04prese-44640, title={The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2}, year={2011}, doi={10.1007/s00249-011-0680-9}, number={4}, volume={40}, issn={0175-7571}, journal={European Biophysics Journal : EBJ}, pages={565--576}, author={Theisgen, Stephan and Thomas, Lars and Schröder, Thomas and Lange, Christian and Kovermann, Michael and Balbach, Jochen and Huster, Daniel} }

Lange, Christian Huster, Daniel Schröder, Thomas eng Schröder, Thomas Guanylate cyclase-activating proteins (GCAPs) are neuronal Ca<sup>2+</sup> sensors that play a central role in shaping the photoreceptor light response and in light adaptation through the Ca<sup>2+</sup>-dependent regulation of the transmembrane retinal guanylate cyclase. GCAPs are N-terminally myristoylated, and the role of the myristoyl moiety is not yet fully understood. While protein lipid chains typically represent membrane anchors, the crystal structure of GCAP-1 showed that the myristoyl chain of the protein is completely buried within a hydrophobic pocket of the protein, which stabilizes the protein structure. Therefore, we address the question of the localization of the myristoyl group of GCAP-2 in the absence and in the presence of lipid membranes as well as DPC detergents (as a membrane substitute amenable to solution state NMR). We investigate membrane binding of both myristoylated and nonmyristoylated GCAP-2 and study the structure and dynamics of the myristoyl moiety of GCAP-2 in the presence of POPC membranes. Further, we address structural alterations within the myristoylated N-terminus of GCAP-2 in the presence of membrane mimetics. Our results suggest that upon membrane binding the myristoyl group is released from the protein interior and inserts into the lipid bilayer. 2019-01-21T12:05:39Z Balbach, Jochen Kovermann, Michael Kovermann, Michael Theisgen, Stephan 2011-04 Thomas, Lars The presence of membranes or micelles induces structural changes of the myristoylated guanylate-cyclase activating protein-2 Thomas, Lars Balbach, Jochen Theisgen, Stephan Huster, Daniel 2019-01-21T12:05:39Z Lange, Christian

This item appears in the following Collection(s)

Search KOPS


Browse

My Account