Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality

Kód výsledku v 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>

Nalezeny alternativní kódy

RIV/61389030:_____/17:00478753

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

<a href="/cs/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Řízení struktury a funkce biomolekul na molekulové úrovni: souhra teorie a experimentu</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2017

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

ACS Central Science

ISSN

2374-7943

e-ISSN

—

Svazek periodika

3

Číslo periodika v rámci svazku

8

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

7

Strana od-do

868-874

Kód UT WoS článku

000408141900011

EID výsledku v databázi Scopus

2-s2.0-85028063042