Unraveling the Impact of Cysteine-to-Serine Mutations on the Structural and Functional Properties of Cu(I)-Binding Proteins

Unraveling the Impact of Cysteine-to-Serine Mutations on the Structural and Functional Properties of Cu(I)-Binding Proteins

Appropriate maintenance of Cu(I) homeostasis is an essential requirement for proper cell function because its misregulation induces the onset of major human diseases and mortality. For this reason, several research efforts have been devoted to dissecting the inner working mechanism of Cu(I)-binding...

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Bibliographic Details
Main Authors: Matic Pavlin, Zena Qasem, Hila Sameach, Lada Gevorkyan-Airapetov, Ida Ritacco, Sharon Ruthstein, Alessandra Magistrato
Format: Article
Language:English
Published: MDPI AG 2019-07-01
Series:International Journal of Molecular Sciences
Subjects:
copper metabolism
serine mutations
Cu(I) affinity
CueR
Atox1
ATP7B
EPR
molecular dynamics
QM/MM
Online Access:https://www.mdpi.com/1422-0067/20/14/3462

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https://www.mdpi.com/1422-0067/20/14/3462

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