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Structure of the human TRPM4 ion channel in a lipid nanodisc.

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Title: Structure of the human TRPM4 ion channel in a lipid nanodisc.
Authors: Autzen, Henriette E., Myasnikov, Alexander G., Campbell, Melody G., Asarnow, Daniel, Julius, David, Yifan Cheng
Source: Science (pre-March 2025). 1/12/2018, Vol. 359 Issue 6372, p228-232. 5p. 4 Color Photographs.
Subjects: TRP channels, Ion channels, Lipids, Calcium, Morphology, Molecular dynamics
Abstract: Transient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular calcium in a voltage-dependent manner but, unlike many other TRP channels, is permeable to monovalent cations only. Here we present two structures of full-length human TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo–electron microscopy. These structures, with and without calcium bound, reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain. The structures correspond to two distinct closed states. Calcium binding induces conformational changes that likely prime the channel for voltage-dependent opening. [ABSTRACT FROM AUTHOR]
Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Psychology and Behavioral Sciences Collection
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DbLabel: Psychology and Behavioral Sciences Collection
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PubTypeId: academicJournal
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  Data: Structure of the human TRPM4 ion channel in a lipid nanodisc.
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  Data: <searchLink fieldCode="AR" term="%22Autzen%2C+Henriette+E%2E%22">Autzen, Henriette E.</searchLink><br /><searchLink fieldCode="AR" term="%22Myasnikov%2C+Alexander+G%2E%22">Myasnikov, Alexander G.</searchLink><br /><searchLink fieldCode="AR" term="%22Campbell%2C+Melody+G%2E%22">Campbell, Melody G.</searchLink><br /><searchLink fieldCode="AR" term="%22Asarnow%2C+Daniel%22">Asarnow, Daniel</searchLink><br /><searchLink fieldCode="AR" term="%22Julius%2C+David%22">Julius, David</searchLink><br /><searchLink fieldCode="AR" term="%22Yifan+Cheng%22">Yifan Cheng</searchLink>
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  Data: <searchLink fieldCode="JN" term="%22Science+%28pre-March+2025%29%22">Science (pre-March 2025)</searchLink>. 1/12/2018, Vol. 359 Issue 6372, p228-232. 5p. 4 Color Photographs.
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  Data: <searchLink fieldCode="DE" term="%22TRP+channels%22">TRP channels</searchLink><br /><searchLink fieldCode="DE" term="%22Ion+channels%22">Ion channels</searchLink><br /><searchLink fieldCode="DE" term="%22Lipids%22">Lipids</searchLink><br /><searchLink fieldCode="DE" term="%22Calcium%22">Calcium</searchLink><br /><searchLink fieldCode="DE" term="%22Morphology%22">Morphology</searchLink><br /><searchLink fieldCode="DE" term="%22Molecular+dynamics%22">Molecular dynamics</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: Transient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular calcium in a voltage-dependent manner but, unlike many other TRP channels, is permeable to monovalent cations only. Here we present two structures of full-length human TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo–electron microscopy. These structures, with and without calcium bound, reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain. The structures correspond to two distinct closed states. Calcium binding induces conformational changes that likely prime the channel for voltage-dependent opening. [ABSTRACT FROM AUTHOR]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Science (pre-March 2025) is the property of American Association for the Advancement of Science and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=pbh&AN=127378535
RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1126/science.aar4510
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      – Code: eng
        Text: English
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      Pagination:
        PageCount: 5
        StartPage: 228
    Subjects:
      – SubjectFull: TRP channels
        Type: general
      – SubjectFull: Ion channels
        Type: general
      – SubjectFull: Lipids
        Type: general
      – SubjectFull: Calcium
        Type: general
      – SubjectFull: Morphology
        Type: general
      – SubjectFull: Molecular dynamics
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      – TitleFull: Structure of the human TRPM4 ion channel in a lipid nanodisc.
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            NameFull: Autzen, Henriette E.
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            NameFull: Myasnikov, Alexander G.
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            NameFull: Campbell, Melody G.
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            NameFull: Asarnow, Daniel
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            NameFull: Julius, David
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              M: 01
              Text: 1/12/2018
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              Y: 2018
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              Value: 359
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