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Naslov:The conformational plasticity of the selectivity filter methionines controls the in-cell Cu(I) uptake through the CTR1 transporter
Avtorji:ID Janoš, Pavel, Consiglio Nazionale delle ricerche/National Research Council (CNR) -IOM c/o International School for Advanced Studies (SISSA/ISAS), via Bonomea 265, 34136Trieste, Italy (Avtor)
ID Aupič, Jana, Consiglio Nazionale delle ricerche/National Research Council (CNR) -IOM c/o International School for Advanced Studies (SISSA/ISAS), via Bonomea 265, 34136Trieste, Italy (Avtor)
ID Ruthstein , Sharon, Department of Chemistry, Faculty of Exact Sciences and the Institute for Nanotechnology and Advanced Materials (BINA), Bar-Ilan University, 5290002, Ramat-Gan, Israel (Avtor)
ID Magistrato, Alessandra, Consiglio Nazionale delle ricerche/National Research Council (CNR) -IOM c/o International School for Advanced Studies (SISSA/ISAS), via Bonomea 265, 34136Trieste, Italy (Avtor)
Datoteke: Gradivo nima datotek, ki so prostodostopne za javnost. Gradivo je morda fizično dosegljivo v knjižnici fakultete, zalogo lahko preverite v COBISS-u. Povezava se odpre v novem oknu
Jezik:Angleški jezik
Vrsta gradiva:Delo ni kategorizirano
Tipologija:1.01 - Izvirni znanstveni članek
Organizacija:UNG - Univerza v Novi Gorici
Opis:Copper is a trace element vital to many cellular functions. Yet its abnormal levels are toxic to cells, provoking a variety of severe diseases. The high affinity copper transporter 1 (CTR1), being the main in-cell copper [Cu(I)] entry route, tightly regulates its cellular uptake via a still elusive mechanism. Here, all-atoms simulations unlock the molecular terms of Cu(I) transport in eukaryotes disclosing that the two methionine (Met) triads, forming the selectivity filter, play an unprecedented dual role both enabling selective Cu(I) transport and regulating its uptake rate thanks to an intimate coupling between the conformational plasticity of their bulky side chains and the number of bound Cu(I) ions. Namely, the Met residues act as a gate reducing the Cu(I) import rate when two ions simultaneously bind to CTR1. This may represent an elegant autoregulatory mechanism through which CTR1 protects the cells from excessively high, and hence toxic, in-cell Cu(I) levels. Overall, our outcomes resolve fundamental questions in CTR1 biology and open new windows of opportunity to tackle diseases associated with an imbalanced copper uptake.
Ključne besede:copper, membrane transporter, molecular dynamics, QM/MM, free energy
Verzija publikacije:Objavljena publikacija
Leto izida:2022
Št. strani:8
Številčenje:3
PID:20.500.12556/RUNG-7602 Novo okno
COBISS.SI-ID:121416195 Novo okno
DOI:DOI: https://doi.org/10.1017/qrd.2022.2 Novo okno
NUK URN:URN:SI:UNG:REP:ZPIXYHWJ
Datum objave v RUNG:15.09.2022
Število ogledov:1496
Število prenosov:0
Metapodatki:XML RDF-CHPDL DC-XML DC-RDF
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Gradivo je del revije

Naslov:QRB discovery
Leto izida:2022

Licence

Licenca:CC BY 4.0, Creative Commons Priznanje avtorstva 4.0 Mednarodna
Povezava:http://creativecommons.org/licenses/by/4.0/deed.sl
Opis:To je standardna licenca Creative Commons, ki daje uporabnikom največ možnosti za nadaljnjo uporabo dela, pri čemer morajo navesti avtorja.
Začetek licenciranja:14.09.2022

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