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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.

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

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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