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Dynamic closed stat...
Dynamic closed states of a ligand-gated ion channel captured by cryo-EM and simulations
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- Rovšnik, Urška (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
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- Zhuang, Yuxuan (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
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- Forsberg, Björn O. (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab),University of Oxford, UK
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- Carroni, Marta (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
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- Yvonnesdotter, Linnea (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
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- Howard, Rebecca J. (författare)
- Stockholms universitet,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab)
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- Lindahl, Erik, 1972- (författare)
- Stockholms universitet,KTH,Biofysik,Science for Life Laboratory, SciLifeLab,Stockholm Univ, Dept Biochem & Biophys, Sci Life Lab, Solna, Sweden.,Institutionen för biokemi och biofysik,Science for Life Laboratory (SciLifeLab),Kungliga Tekniska Högskolan Royal Institute of Technology, Sweden
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(creator_code:org_t)
- 2021-07-01
- 2021
- Engelska.
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Ingår i: Life Science Alliance. - : Life Science Alliance, LLC. - 2575-1077. ; 4:8
- Relaterad länk:
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https://doi.org/10.2...
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https://www.life-sci...
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https://urn.kb.se/re...
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https://doi.org/10.2...
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https://urn.kb.se/re...
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Abstract
Ämnesord
Stäng
- Ligand-gated ion channels are critical mediators of electrochemical signal transduction across evolution. Biophysical and pharmacological characterization of these receptor proteins relies on high-quality structures in multiple, subtly distinct functional states. However, structural data in this family remain limited, particularly for resting and intermediate states on the activation pathway. Here, we report cryo-electr on microscopy (cryo-EM) structures of the proton-activated Gloeobacter violaceus ligandgated ion channel (GLIC) under three pH conditions. Decreased pH was associated with improved resolution and side chain rearrangements at the subunit/domain interface, particularly involving functionally important residues in the beta 1-beta 2 and M2-M3 loops. Molecular dynamics simulations substantiated flexibility in the closed-channel extracellular domains relative to the transmembrane ones and supported electrostatic remodeling around E35 and E243 in proton-induced gating. Exploration of secondary cryoEM classes further indicated a low-pH population with an expanded pore. These results allow us to define distinct protonation and activation steps in pH-stimulated conformational cycling in GLIC, including interfacial rearrangements largely conserved in the pentameric channel family.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences (hsv//eng)
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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