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Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality

Tutkimustuotosvertaisarvioitu

Standard

Membrane Binding of Recoverin : From Mechanistic Understanding to Biological Functionality. / Timr, Štěpán; Pleskot, Roman; Kadlec, Jan; Kohagen, Miriam; Magarkar, Aniket; Jungwirth, Pavel.

julkaisussa: ACS Central Science, Vuosikerta 3, Nro 8, 23.08.2017, s. 868-874.

Tutkimustuotosvertaisarvioitu

Harvard

Timr, Š, Pleskot, R, Kadlec, J, Kohagen, M, Magarkar, A & Jungwirth, P 2017, 'Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality', ACS Central Science, Vuosikerta. 3, Nro 8, Sivut 868-874. https://doi.org/10.1021/acscentsci.7b00210

APA

Timr, Š., Pleskot, R., Kadlec, J., Kohagen, M., Magarkar, A., & Jungwirth, P. (2017). Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality. ACS Central Science, 3(8), 868-874. https://doi.org/10.1021/acscentsci.7b00210

Vancouver

Timr Š, Pleskot R, Kadlec J, Kohagen M, Magarkar A, Jungwirth P. Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality. ACS Central Science. 2017 elo 23;3(8):868-874. https://doi.org/10.1021/acscentsci.7b00210

Author

Timr, Štěpán ; Pleskot, Roman ; Kadlec, Jan ; Kohagen, Miriam ; Magarkar, Aniket ; Jungwirth, Pavel. / Membrane Binding of Recoverin : From Mechanistic Understanding to Biological Functionality. Julkaisussa: ACS Central Science. 2017 ; Vuosikerta 3, Nro 8. Sivut 868-874.

Bibtex - Lataa

@article{ba4de84f18e9430db92efb946415a9ea,
title = "Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality",
abstract = "Recoverin is a neuronal calcium sensor involved in vision adaptation that reversibly associates with cellular membranes via its calcium-activated myristoyl switch. While experimental evidence shows that the myristoyl group significantly enhances membrane affinity of this protein, molecular details of the binding process are still under debate. Here, we present results of extensive molecular dynamics simulations of recoverin in the proximity of a phospholipid bilayer. We capture multiple events of spontaneous membrane insertion of the myristoyl moiety and confirm its critical role in the membrane binding. Moreover, we observe that the binding strongly depends on the conformation of the N-terminal domain. We propose that a suitable conformation of the N-terminal domain can be stabilized by the disordered C-terminal segment or by binding of the target enzyme, i.e., rhodopsin kinase. Finally, we find that the presence of negatively charged lipids in the bilayer stabilizes a physiologically functional orientation of the membrane-bound recoverin.",
author = "Štěp{\'a}n Timr and Roman Pleskot and Jan Kadlec and Miriam Kohagen and Aniket Magarkar and Pavel Jungwirth",
year = "2017",
month = "8",
day = "23",
doi = "10.1021/acscentsci.7b00210",
language = "English",
volume = "3",
pages = "868--874",
journal = "ACS Central Science",
issn = "2374-7943",
publisher = "American Chemical Society",
number = "8",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Membrane Binding of Recoverin

T2 - From Mechanistic Understanding to Biological Functionality

AU - Timr, Štěpán

AU - Pleskot, Roman

AU - Kadlec, Jan

AU - Kohagen, Miriam

AU - Magarkar, Aniket

AU - Jungwirth, Pavel

PY - 2017/8/23

Y1 - 2017/8/23

N2 - Recoverin is a neuronal calcium sensor involved in vision adaptation that reversibly associates with cellular membranes via its calcium-activated myristoyl switch. While experimental evidence shows that the myristoyl group significantly enhances membrane affinity of this protein, molecular details of the binding process are still under debate. Here, we present results of extensive molecular dynamics simulations of recoverin in the proximity of a phospholipid bilayer. We capture multiple events of spontaneous membrane insertion of the myristoyl moiety and confirm its critical role in the membrane binding. Moreover, we observe that the binding strongly depends on the conformation of the N-terminal domain. We propose that a suitable conformation of the N-terminal domain can be stabilized by the disordered C-terminal segment or by binding of the target enzyme, i.e., rhodopsin kinase. Finally, we find that the presence of negatively charged lipids in the bilayer stabilizes a physiologically functional orientation of the membrane-bound recoverin.

AB - Recoverin is a neuronal calcium sensor involved in vision adaptation that reversibly associates with cellular membranes via its calcium-activated myristoyl switch. While experimental evidence shows that the myristoyl group significantly enhances membrane affinity of this protein, molecular details of the binding process are still under debate. Here, we present results of extensive molecular dynamics simulations of recoverin in the proximity of a phospholipid bilayer. We capture multiple events of spontaneous membrane insertion of the myristoyl moiety and confirm its critical role in the membrane binding. Moreover, we observe that the binding strongly depends on the conformation of the N-terminal domain. We propose that a suitable conformation of the N-terminal domain can be stabilized by the disordered C-terminal segment or by binding of the target enzyme, i.e., rhodopsin kinase. Finally, we find that the presence of negatively charged lipids in the bilayer stabilizes a physiologically functional orientation of the membrane-bound recoverin.

U2 - 10.1021/acscentsci.7b00210

DO - 10.1021/acscentsci.7b00210

M3 - Article

VL - 3

SP - 868

EP - 874

JO - ACS Central Science

JF - ACS Central Science

SN - 2374-7943

IS - 8

ER -