Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00478298" target="_blank" >RIV/61388963:_____/17:00478298 - isvavai.cz</a>
Alternative codes found
RIV/61389030:_____/17:00478753
Result on the web
<a href="http://pubs.acs.org/doi/full/10.1021/acscentsci.7b00210" target="_blank" >http://pubs.acs.org/doi/full/10.1021/acscentsci.7b00210</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acscentsci.7b00210" target="_blank" >10.1021/acscentsci.7b00210</a>
Alternative languages
Result language
angličtina
Original language name
Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2017
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
ACS Central Science
ISSN
2374-7943
e-ISSN
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Volume of the periodical
3
Issue of the periodical within the volume
8
Country of publishing house
US - UNITED STATES
Number of pages
7
Pages from-to
868-874
UT code for WoS article
000408141900011
EID of the result in the Scopus database
2-s2.0-85028063042