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LIIT-ChR2

Structural and mechanistic study of ion transport in Channelrhodopsin-2

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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.

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

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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