Energetic landscape of polycystin channel gating
Members of the polycystin family (PKD2 and PKD2L1) of transient receptor potential (TRP) channels conduct Ca 2+ and depolarizing monovalent cations. Variants in PKD2 cause autosomal dominant polycystic kidney disease (ADPKD) in humans, whereas loss of PKD2L1 expression causes seizure susceptibility...
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| Veröffentlicht in: | EMBO reports 2023-07, Vol.24 (7), p.e56783-n/a |
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| creator | Ng, Leo CT Harris, Brandon J Larmore, Megan Ta, My C Vien, Thuy N Tokars, Valerie L Yarov‐Yarovoy, Vladimir DeCaen, Paul G |
| description | Members of the polycystin family (PKD2 and PKD2L1) of transient receptor potential (TRP) channels conduct Ca
2+
and depolarizing monovalent cations. Variants in PKD2 cause autosomal dominant polycystic kidney disease (ADPKD) in humans, whereas loss of PKD2L1 expression causes seizure susceptibility in mice. Understanding structural and functional regulation of these channels will provide the basis for interpreting their molecular dysregulation in disease states. However, the complete structures of polycystins are unresolved, as are the conformational changes regulating their conductive states. To provide a holistic understanding of the polycystin gating cycle, we use computational prediction tools to model missing PKD2L1 structural motifs and evaluate more than 150 mutations in an unbiased mutagenic functional screen of the entire pore module. Our results provide an energetic landscape of the polycystin pore, which enumerates gating sensitive sites and interactions required for opening, inactivation, and subsequent desensitization. These findings identify the external pore helices and specific cross‐domain interactions as critical structural regulators controlling the polycystin ion channel conductive and nonconductive states.
Synopsis
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel.
External pore helix interactions regulate the polycystin channel opening.
Opening the inner and outer pore gates are energetically coupled.
Inactivation and desensitized are structurally related states controlled by specific inter‐subunit interactions between the pore helix 1 and sixth transmembrane segment.
Graphical Abstract
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel. |
| doi_str_mv | 10.15252/embr.202356783 |
| format | Article |
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2+
and depolarizing monovalent cations. Variants in PKD2 cause autosomal dominant polycystic kidney disease (ADPKD) in humans, whereas loss of PKD2L1 expression causes seizure susceptibility in mice. Understanding structural and functional regulation of these channels will provide the basis for interpreting their molecular dysregulation in disease states. However, the complete structures of polycystins are unresolved, as are the conformational changes regulating their conductive states. To provide a holistic understanding of the polycystin gating cycle, we use computational prediction tools to model missing PKD2L1 structural motifs and evaluate more than 150 mutations in an unbiased mutagenic functional screen of the entire pore module. Our results provide an energetic landscape of the polycystin pore, which enumerates gating sensitive sites and interactions required for opening, inactivation, and subsequent desensitization. These findings identify the external pore helices and specific cross‐domain interactions as critical structural regulators controlling the polycystin ion channel conductive and nonconductive states.
Synopsis
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel.
External pore helix interactions regulate the polycystin channel opening.
Opening the inner and outer pore gates are energetically coupled.
Inactivation and desensitized are structurally related states controlled by specific inter‐subunit interactions between the pore helix 1 and sixth transmembrane segment.
Graphical Abstract
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel.</description><identifier>ISSN: 1469-221X</identifier><identifier>ISSN: 1469-3178</identifier><identifier>EISSN: 1469-3178</identifier><identifier>DOI: 10.15252/embr.202356783</identifier><identifier>PMID: 37158562</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Brain ; calcium ; Calcium channels ; Calcium Channels - metabolism ; Calcium ions ; Cations ; Channel gating ; Channel opening ; Channelopathy ; Computational neuroscience ; Conformation (molecular) ; Deactivation ; Depolarization ; Desensitization ; EMBO24 ; Helices ; Humans ; Inactivation ; Ion channels ; Ion Transport ; Kidney diseases ; Kidneys ; Life Sciences ; Membrane channels ; Mice ; Modules ; Mutation ; Pathogenesis ; Polycystic kidney ; polycystic kidney disease ; polycystins ; Receptors, Cell Surface - metabolism ; Seizures ; Signal Transduction ; Software ; structural biology ; Structure-function relationships ; Transient Receptor Potential Channels - genetics ; Transient receptor potential proteins ; TRP channels ; TRPP Cation Channels - chemistry</subject><ispartof>EMBO reports, 2023-07, Vol.24 (7), p.e56783-n/a</ispartof><rights>The Author(s) 2023</rights><rights>2023 The Authors. Published under the terms of the CC BY NC ND 4.0 license.</rights><rights>2023. This article is published under http://creativecommons.org/licenses/by-nc-nd/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4683-fd4a736b86b0b57fa8e787978ed29c33ac37a28450e1adf337af637b5b68274b3</cites><orcidid>0000-0002-0492-5460 ; 0000-0003-3894-0180 ; 0000-0001-8776-983X ; 0000-0002-2619-3969 ; 0000-0002-2325-4834</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10328073/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC10328073/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,1416,1432,27922,27923,41118,42187,45572,45573,46407,46831,51574,53789,53791</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37158562$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ng, Leo CT</creatorcontrib><creatorcontrib>Harris, Brandon J</creatorcontrib><creatorcontrib>Larmore, Megan</creatorcontrib><creatorcontrib>Ta, My C</creatorcontrib><creatorcontrib>Vien, Thuy N</creatorcontrib><creatorcontrib>Tokars, Valerie L</creatorcontrib><creatorcontrib>Yarov‐Yarovoy, Vladimir</creatorcontrib><creatorcontrib>DeCaen, Paul G</creatorcontrib><title>Energetic landscape of polycystin channel gating</title><title>EMBO reports</title><addtitle>EMBO Rep</addtitle><addtitle>EMBO Rep</addtitle><description>Members of the polycystin family (PKD2 and PKD2L1) of transient receptor potential (TRP) channels conduct Ca
2+
and depolarizing monovalent cations. Variants in PKD2 cause autosomal dominant polycystic kidney disease (ADPKD) in humans, whereas loss of PKD2L1 expression causes seizure susceptibility in mice. Understanding structural and functional regulation of these channels will provide the basis for interpreting their molecular dysregulation in disease states. However, the complete structures of polycystins are unresolved, as are the conformational changes regulating their conductive states. To provide a holistic understanding of the polycystin gating cycle, we use computational prediction tools to model missing PKD2L1 structural motifs and evaluate more than 150 mutations in an unbiased mutagenic functional screen of the entire pore module. Our results provide an energetic landscape of the polycystin pore, which enumerates gating sensitive sites and interactions required for opening, inactivation, and subsequent desensitization. These findings identify the external pore helices and specific cross‐domain interactions as critical structural regulators controlling the polycystin ion channel conductive and nonconductive states.
Synopsis
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel.
External pore helix interactions regulate the polycystin channel opening.
Opening the inner and outer pore gates are energetically coupled.
Inactivation and desensitized are structurally related states controlled by specific inter‐subunit interactions between the pore helix 1 and sixth transmembrane segment.
Graphical Abstract
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel.</description><subject>Animals</subject><subject>Brain</subject><subject>calcium</subject><subject>Calcium channels</subject><subject>Calcium Channels - metabolism</subject><subject>Calcium ions</subject><subject>Cations</subject><subject>Channel gating</subject><subject>Channel opening</subject><subject>Channelopathy</subject><subject>Computational neuroscience</subject><subject>Conformation (molecular)</subject><subject>Deactivation</subject><subject>Depolarization</subject><subject>Desensitization</subject><subject>EMBO24</subject><subject>Helices</subject><subject>Humans</subject><subject>Inactivation</subject><subject>Ion channels</subject><subject>Ion Transport</subject><subject>Kidney diseases</subject><subject>Kidneys</subject><subject>Life Sciences</subject><subject>Membrane channels</subject><subject>Mice</subject><subject>Modules</subject><subject>Mutation</subject><subject>Pathogenesis</subject><subject>Polycystic kidney</subject><subject>polycystic kidney disease</subject><subject>polycystins</subject><subject>Receptors, Cell Surface - metabolism</subject><subject>Seizures</subject><subject>Signal Transduction</subject><subject>Software</subject><subject>structural biology</subject><subject>Structure-function relationships</subject><subject>Transient Receptor Potential Channels - genetics</subject><subject>Transient receptor potential proteins</subject><subject>TRP channels</subject><subject>TRPP Cation Channels - chemistry</subject><issn>1469-221X</issn><issn>1469-3178</issn><issn>1469-3178</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>EIF</sourceid><recordid>eNqFkUtLAzEUhYMoVqtrdzLgxk3bPCaT1I1oqQ-oCKLgLmQyd6ZTppmatMr8e6OttQriIiSXfOfk3FyEjgjuEk457cE0dV2KKeOJkGwL7ZE46XcYEXJ7daaUPLfQvvcTjDHvC7mLWkwQLnlC9xAeWnAFzEsTVdpm3ugZRHUezeqqMY2flzYyY20tVFGhQ1UcoJ1cVx4OV3sbPV0NHwc3ndH99e3gYtQxcSJZJ89iLViSyiTFKRe5liCkCK9DRvuGMW2Y0FTGHAPRWc5ClSdMpDxNJBVxytrofOk7W6RTyAzYudOVmrlyql2jal2qnze2HKuiflUEMyqxYMHhdOXg6pcF-Lmalt5AFfqEeuEVlYRwgcMK6MkvdFIvnA39BYrFJBYUx4HqLSnjau8d5Os0BKvPcaiPcaj1OILieLOJNf_1_wE4WwJvZQXNf35qeHf5sOmOl2IfdLYA9536r0Dvy0emuA</recordid><startdate>20230705</startdate><enddate>20230705</enddate><creator>Ng, Leo CT</creator><creator>Harris, Brandon J</creator><creator>Larmore, Megan</creator><creator>Ta, My C</creator><creator>Vien, Thuy N</creator><creator>Tokars, Valerie L</creator><creator>Yarov‐Yarovoy, Vladimir</creator><creator>DeCaen, Paul G</creator><general>Nature Publishing Group UK</general><general>Blackwell Publishing Ltd</general><general>John Wiley and Sons Inc</general><scope>C6C</scope><scope>24P</scope><scope>WIN</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7T5</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-0492-5460</orcidid><orcidid>https://orcid.org/0000-0003-3894-0180</orcidid><orcidid>https://orcid.org/0000-0001-8776-983X</orcidid><orcidid>https://orcid.org/0000-0002-2619-3969</orcidid><orcidid>https://orcid.org/0000-0002-2325-4834</orcidid></search><sort><creationdate>20230705</creationdate><title>Energetic landscape of polycystin channel gating</title><author>Ng, Leo CT ; Harris, Brandon J ; Larmore, Megan ; Ta, My C ; Vien, Thuy N ; Tokars, Valerie L ; Yarov‐Yarovoy, Vladimir ; DeCaen, Paul G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4683-fd4a736b86b0b57fa8e787978ed29c33ac37a28450e1adf337af637b5b68274b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Animals</topic><topic>Brain</topic><topic>calcium</topic><topic>Calcium channels</topic><topic>Calcium Channels - metabolism</topic><topic>Calcium ions</topic><topic>Cations</topic><topic>Channel gating</topic><topic>Channel opening</topic><topic>Channelopathy</topic><topic>Computational neuroscience</topic><topic>Conformation (molecular)</topic><topic>Deactivation</topic><topic>Depolarization</topic><topic>Desensitization</topic><topic>EMBO24</topic><topic>Helices</topic><topic>Humans</topic><topic>Inactivation</topic><topic>Ion channels</topic><topic>Ion Transport</topic><topic>Kidney diseases</topic><topic>Kidneys</topic><topic>Life Sciences</topic><topic>Membrane channels</topic><topic>Mice</topic><topic>Modules</topic><topic>Mutation</topic><topic>Pathogenesis</topic><topic>Polycystic kidney</topic><topic>polycystic kidney disease</topic><topic>polycystins</topic><topic>Receptors, Cell Surface - metabolism</topic><topic>Seizures</topic><topic>Signal Transduction</topic><topic>Software</topic><topic>structural biology</topic><topic>Structure-function relationships</topic><topic>Transient Receptor Potential Channels - genetics</topic><topic>Transient receptor potential proteins</topic><topic>TRP channels</topic><topic>TRPP Cation Channels - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ng, Leo CT</creatorcontrib><creatorcontrib>Harris, Brandon J</creatorcontrib><creatorcontrib>Larmore, Megan</creatorcontrib><creatorcontrib>Ta, My C</creatorcontrib><creatorcontrib>Vien, Thuy N</creatorcontrib><creatorcontrib>Tokars, Valerie L</creatorcontrib><creatorcontrib>Yarov‐Yarovoy, Vladimir</creatorcontrib><creatorcontrib>DeCaen, Paul G</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Wiley Online Library Open Access</collection><collection>Wiley Free Content</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>EMBO reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ng, Leo CT</au><au>Harris, Brandon J</au><au>Larmore, Megan</au><au>Ta, My C</au><au>Vien, Thuy N</au><au>Tokars, Valerie L</au><au>Yarov‐Yarovoy, Vladimir</au><au>DeCaen, Paul G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Energetic landscape of polycystin channel gating</atitle><jtitle>EMBO reports</jtitle><stitle>EMBO Rep</stitle><addtitle>EMBO Rep</addtitle><date>2023-07-05</date><risdate>2023</risdate><volume>24</volume><issue>7</issue><spage>e56783</spage><epage>n/a</epage><pages>e56783-n/a</pages><issn>1469-221X</issn><issn>1469-3178</issn><eissn>1469-3178</eissn><abstract>Members of the polycystin family (PKD2 and PKD2L1) of transient receptor potential (TRP) channels conduct Ca
2+
and depolarizing monovalent cations. Variants in PKD2 cause autosomal dominant polycystic kidney disease (ADPKD) in humans, whereas loss of PKD2L1 expression causes seizure susceptibility in mice. Understanding structural and functional regulation of these channels will provide the basis for interpreting their molecular dysregulation in disease states. However, the complete structures of polycystins are unresolved, as are the conformational changes regulating their conductive states. To provide a holistic understanding of the polycystin gating cycle, we use computational prediction tools to model missing PKD2L1 structural motifs and evaluate more than 150 mutations in an unbiased mutagenic functional screen of the entire pore module. Our results provide an energetic landscape of the polycystin pore, which enumerates gating sensitive sites and interactions required for opening, inactivation, and subsequent desensitization. These findings identify the external pore helices and specific cross‐domain interactions as critical structural regulators controlling the polycystin ion channel conductive and nonconductive states.
Synopsis
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel.
External pore helix interactions regulate the polycystin channel opening.
Opening the inner and outer pore gates are energetically coupled.
Inactivation and desensitized are structurally related states controlled by specific inter‐subunit interactions between the pore helix 1 and sixth transmembrane segment.
Graphical Abstract
Conformational changes that open polycystins are critical for their ion channel function in brain and kidney. Results from an unbiased functional screen of the entire polycystin pore module and AI‐driven structural modeling provide an energetic landscape while enumerate gating‐sensitive sites controlling the conductive states of the channel.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>37158562</pmid><doi>10.15252/embr.202356783</doi><tpages>18</tpages><orcidid>https://orcid.org/0000-0002-0492-5460</orcidid><orcidid>https://orcid.org/0000-0003-3894-0180</orcidid><orcidid>https://orcid.org/0000-0001-8776-983X</orcidid><orcidid>https://orcid.org/0000-0002-2619-3969</orcidid><orcidid>https://orcid.org/0000-0002-2325-4834</orcidid><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Springer Nature OA Free Journals; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Wiley Online Library All Journals; PubMed Central |
| subjects | Animals Brain calcium Calcium channels Calcium Channels - metabolism Calcium ions Cations Channel gating Channel opening Channelopathy Computational neuroscience Conformation (molecular) Deactivation Depolarization Desensitization EMBO24 Helices Humans Inactivation Ion channels Ion Transport Kidney diseases Kidneys Life Sciences Membrane channels Mice Modules Mutation Pathogenesis Polycystic kidney polycystic kidney disease polycystins Receptors, Cell Surface - metabolism Seizures Signal Transduction Software structural biology Structure-function relationships Transient Receptor Potential Channels - genetics Transient receptor potential proteins TRP channels TRPP Cation Channels - chemistry |
| title | Energetic landscape of polycystin channel gating |
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