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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

  • 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