Structure and topology of the transmembrane domain 4 of the divalent metal transporter in membrane-mimetic environments
β 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. Diseaseβcausing 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
## Abstract Membrane protein Nramp1 (natural resistanceβassociated macrophage protein 1) is a pHβdependent 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