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Structure and topology of the transmembrane domain 4 of the divalent metal transporter in membrane-mimetic environments

✍ Scribed by Hongyan Li; Fei Li; Zhong Ming Qian; Hongzhe Sun


Book ID
110915038
Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
562 KB
Volume
271
Category
Article
ISSN
1432-1327

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## Abstract DMT1, also known as Nramp2, is an iron transporter, and belongs to the family of Nramp proteins. Disease‐causing mutations both in Nramp1 and Nramp2 occurring at the conserved two adjacent glycine residues located within the fourth transmembrane domain (TM4) suggest that TM4 may serve a

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## Abstract Membrane protein Nramp1 (natural resistance‐associated macrophage protein 1) is a pH‐dependent divalent metal cation transporter that regulates macrophage activation in infectious and autoimmune diseases. A naturally occurring glycine to aspartic acid substitution at position 169 (G169D