Cryo-EM structure of the human concentrative nucleoside transporter CNT3.

Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determin...
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Autor*in:	Yanxia Zhou [verfasserIn] Lianghuan Liao [verfasserIn] Chen Wang [verfasserIn] Jialu Li [verfasserIn] Pengliang Chi [verfasserIn] Qingjie Xiao [verfasserIn] Qingting Liu [verfasserIn] Li Guo [verfasserIn] Linfeng Sun [verfasserIn] Dong Deng [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Übergeordnetes Werk:	In: PLoS Biology - Public Library of Science (PLoS), 2003, 18(2020), 8, p e3000790
Übergeordnetes Werk:	volume:18 ; year:2020 ; number:8, p e3000790

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.1371/journal.pbio.3000790

Katalog-ID:	DOAJ004657144

Internformat


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520			\|a Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs.
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author_variant	y z yz l l ll c w cw j l jl p c pc q x qx q l ql l g lg l s ls d d dd
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allfields	10.1371/journal.pbio.3000790 doi (DE-627)DOAJ004657144 (DE-599)DOAJab912d7e4700462a819314c1390a2ee5 DE-627 ger DE-627 rakwb eng QH301-705.5 Yanxia Zhou verfasserin aut Cryo-EM structure of the human concentrative nucleoside transporter CNT3. 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs. Biology (General) Lianghuan Liao verfasserin aut Chen Wang verfasserin aut Jialu Li verfasserin aut Pengliang Chi verfasserin aut Qingjie Xiao verfasserin aut Qingting Liu verfasserin aut Li Guo verfasserin aut Linfeng Sun verfasserin aut Dong Deng verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 18(2020), 8, p e3000790 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:18 year:2020 number:8, p e3000790 https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/article/ab912d7e4700462a819314c1390a2ee5 kostenfrei https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 8, p e3000790
spelling	10.1371/journal.pbio.3000790 doi (DE-627)DOAJ004657144 (DE-599)DOAJab912d7e4700462a819314c1390a2ee5 DE-627 ger DE-627 rakwb eng QH301-705.5 Yanxia Zhou verfasserin aut Cryo-EM structure of the human concentrative nucleoside transporter CNT3. 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs. Biology (General) Lianghuan Liao verfasserin aut Chen Wang verfasserin aut Jialu Li verfasserin aut Pengliang Chi verfasserin aut Qingjie Xiao verfasserin aut Qingting Liu verfasserin aut Li Guo verfasserin aut Linfeng Sun verfasserin aut Dong Deng verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 18(2020), 8, p e3000790 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:18 year:2020 number:8, p e3000790 https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/article/ab912d7e4700462a819314c1390a2ee5 kostenfrei https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 8, p e3000790
allfields_unstemmed	10.1371/journal.pbio.3000790 doi (DE-627)DOAJ004657144 (DE-599)DOAJab912d7e4700462a819314c1390a2ee5 DE-627 ger DE-627 rakwb eng QH301-705.5 Yanxia Zhou verfasserin aut Cryo-EM structure of the human concentrative nucleoside transporter CNT3. 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs. Biology (General) Lianghuan Liao verfasserin aut Chen Wang verfasserin aut Jialu Li verfasserin aut Pengliang Chi verfasserin aut Qingjie Xiao verfasserin aut Qingting Liu verfasserin aut Li Guo verfasserin aut Linfeng Sun verfasserin aut Dong Deng verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 18(2020), 8, p e3000790 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:18 year:2020 number:8, p e3000790 https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/article/ab912d7e4700462a819314c1390a2ee5 kostenfrei https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 8, p e3000790
allfieldsGer	10.1371/journal.pbio.3000790 doi (DE-627)DOAJ004657144 (DE-599)DOAJab912d7e4700462a819314c1390a2ee5 DE-627 ger DE-627 rakwb eng QH301-705.5 Yanxia Zhou verfasserin aut Cryo-EM structure of the human concentrative nucleoside transporter CNT3. 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs. Biology (General) Lianghuan Liao verfasserin aut Chen Wang verfasserin aut Jialu Li verfasserin aut Pengliang Chi verfasserin aut Qingjie Xiao verfasserin aut Qingting Liu verfasserin aut Li Guo verfasserin aut Linfeng Sun verfasserin aut Dong Deng verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 18(2020), 8, p e3000790 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:18 year:2020 number:8, p e3000790 https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/article/ab912d7e4700462a819314c1390a2ee5 kostenfrei https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 8, p e3000790
allfieldsSound	10.1371/journal.pbio.3000790 doi (DE-627)DOAJ004657144 (DE-599)DOAJab912d7e4700462a819314c1390a2ee5 DE-627 ger DE-627 rakwb eng QH301-705.5 Yanxia Zhou verfasserin aut Cryo-EM structure of the human concentrative nucleoside transporter CNT3. 2020 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs. Biology (General) Lianghuan Liao verfasserin aut Chen Wang verfasserin aut Jialu Li verfasserin aut Pengliang Chi verfasserin aut Qingjie Xiao verfasserin aut Qingting Liu verfasserin aut Li Guo verfasserin aut Linfeng Sun verfasserin aut Dong Deng verfasserin aut In PLoS Biology Public Library of Science (PLoS), 2003 18(2020), 8, p e3000790 (DE-627)373755597 (DE-600)2126773-X 15457885 nnns volume:18 year:2020 number:8, p e3000790 https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/article/ab912d7e4700462a819314c1390a2ee5 kostenfrei https://doi.org/10.1371/journal.pbio.3000790 kostenfrei https://doaj.org/toc/1544-9173 Journal toc kostenfrei https://doaj.org/toc/1545-7885 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2031 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2522 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 18 2020 8, p e3000790
language	English
source	In PLoS Biology 18(2020), 8, p e3000790 volume:18 year:2020 number:8, p e3000790
sourceStr	In PLoS Biology 18(2020), 8, p e3000790 volume:18 year:2020 number:8, p e3000790
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	Biology (General)
isfreeaccess_bool	true
container_title	PLoS Biology
authorswithroles_txt_mv	Yanxia Zhou @@aut@@ Lianghuan Liao @@aut@@ Chen Wang @@aut@@ Jialu Li @@aut@@ Pengliang Chi @@aut@@ Qingjie Xiao @@aut@@ Qingting Liu @@aut@@ Li Guo @@aut@@ Linfeng Sun @@aut@@ Dong Deng @@aut@@
publishDateDaySort_date	2020-01-01T00:00:00Z
hierarchy_top_id	373755597
id	DOAJ004657144
language_de	englisch
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callnumber-first	Q - Science
author	Yanxia Zhou
spellingShingle	Yanxia Zhou misc QH301-705.5 misc Biology (General) Cryo-EM structure of the human concentrative nucleoside transporter CNT3.
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topic_title	QH301-705.5 Cryo-EM structure of the human concentrative nucleoside transporter CNT3
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title	Cryo-EM structure of the human concentrative nucleoside transporter CNT3.
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title_full	Cryo-EM structure of the human concentrative nucleoside transporter CNT3
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author_browse	Yanxia Zhou Lianghuan Liao Chen Wang Jialu Li Pengliang Chi Qingjie Xiao Qingting Liu Li Guo Linfeng Sun Dong Deng
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title_sort	cryo-em structure of the human concentrative nucleoside transporter cnt3
callnumber	QH301-705.5
title_auth	Cryo-EM structure of the human concentrative nucleoside transporter CNT3.
abstract	Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs.
abstractGer	Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs.
abstract_unstemmed	Concentrative nucleoside transporters (CNTs), members of the solute carrier (SLC) 28 transporter family, facilitate the salvage of nucleosides and therapeutic nucleoside derivatives across the plasma membrane. Despite decades of investigation, the structures of human CNTs remain unknown. We determined the cryogenic electron microscopy (cryo-EM) structure of human CNT (hCNT) 3 at an overall resolution of 3.6 Å. As with its bacterial homologs, hCNT3 presents a trimeric architecture with additional N-terminal transmembrane helices to stabilize the conserved central domains. The conserved binding sites for the substrate and sodium ions unravel the selective nucleoside transport and distinct coupling mechanism. Structural comparison of hCNT3 with bacterial homologs indicates that hCNT3 is stabilized in an inward-facing conformation. This study provides the molecular determinants for the transport mechanism of hCNTs and potentially facilitates the design of nucleoside drugs.
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container_issue	8, p e3000790
title_short	Cryo-EM structure of the human concentrative nucleoside transporter CNT3.
url	https://doi.org/10.1371/journal.pbio.3000790 https://doaj.org/article/ab912d7e4700462a819314c1390a2ee5 https://doaj.org/toc/1544-9173 https://doaj.org/toc/1545-7885
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Cryo-EM structure of the human concentrative nucleoside transporter CNT3.

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