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LIIT-ChR2

Structural and mechanistic study of ion transport in Channelrhodopsin-2

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EC-Contrib. €

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 Outcomes and results

 LIIT-ChR2 project word cloud

Explore the words cloud of the LIIT-ChR2 project. It provides you a very rough idea of what is the project "LIIT-ChR2" about.

retinas    found    spectroscopic    turn    ray    force    qm    depolarized    groups    aring    sampling    quantum    sensory    enhanced    validated    transient    green    model    closely    map    projection    hence    light    microscopy    host    opens    pass    structures    activation    moiety    contrast    optogenetics    photochemical    group    elucidating    mechanisms    channelrhodopsin    neurons    desensitized    conformational    protein    cycle    damaged    rhodopsin    experimental    electron    function    matching    free    bayesian    algae    little    transport    channelrhodopsins    hoc    absorbance    observations    closed    molecular    evidences    brain    mixture    energy    biophysics    dark    channel    mechanics    close    chimera    contains    disorders    chr2    theoretical    opening    restore    retinal    simulated    action    sensitivity    illumination    ad    cryo    species    environment    mechanism    expressing    ions    channels    inactivation    bacteriorhodopsins    neuronal    circuits    chr1    halorhodopsins    induces    proteins    structural    photoreceptors    ion    limited    reversibly    visual    structure    locations    mm   

Project "LIIT-ChR2" data sheet

The following table provides information about the project.

Coordinator		 MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV 

Organization address
address: HOFGARTENSTRASSE 8
city: MUENCHEN
postcode: 80539
website: n.a.

contact info
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.
 Coordinator Country Germany [DE]
 Project website http://www.biophys.mpg.de/en/tb/channelrhodopsin-2.html
 Total cost 159˙460 €
 EC max contribution 159˙460 € (100%)
 Programme 1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility)
 Code Call H2020-MSCA-IF-2014
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2015
 Duration (year-month-day) from 2015-04-01   to  2017-03-31

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV DE (MUENCHEN) coordinator 159˙460.00

Map

 Project objective

Channelrhodopsins are type-I rhodopsin proteins found in green algae that function as sensory photoreceptors and turn into ion channels under illumination. Upon light absorbance, the retinal moiety induces a conformational change on the protein that opens a channel through which ions can pass. Neurons expressing channelrhodopsin-2 (ChR2) can be depolarized rapidly and reversibly by illumination, hence allowing control of the activation/inactivation of neurons in specific locations of the brain. For this reason, ChR2 has been used widely in optogenetics to study neuronal circuits and disorders in the brain, and to restore light sensitivity and visual capabilities in damaged retinas. However, in contrast to closely related bacteriorhodopsins or halorhodopsins, very little is known about their structure, light cycle and mechanism of action. The current structural evidences of ChR2 is limited to 1) the 6 Å projection map obtained by cryo-electron microscopy that contains a mixture of light (open channel) and dark (closed channel) states; and 2) the 2.3 Å X-ray structure of the dark state of a ChR1/ChR2 chimera. In the present proposal, we aim at elucidating the structure, properties and mechanism of action of the transient species of ChR2 during its photochemical cycle by means of theoretical methods and in close collaboration with the experimental biophysics groups of the host institute. The mechanisms of ion transport and channel opening will be simulated by enhanced sampling and free energy methods. Specific quantum-mechanics/molecular-mechanics (QM/MM) force matching force field will be generated ad hoc for the retinal moiety in the ChR2 environment. The model structures generated for the closed, open, and desensitized states will be validated 1) by comparison of the QM/MM spectroscopic properties of the model with experimental observations; and 2) by comparison to electron microscopy structures using a Bayesian analysis method recently developed in the host group.

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