NMR structures and orientation of the fourth transmembrane domain of the rat divalent metal transporter (DMT1) with G185D mutation in SDS micelles
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Summary
The high‐resolution structures of a synthetic peptide corresponding to the sequence of the fourth transmembrane domain of rat DMT1 with G185D mutation are determined, in membrane‐mimetic environments (e.g., SDS micelles) using NMR spectroscopy and distance‐geometry/simulated annealing calculations.
- Type
- article
- Published
- 2005-03-01
- Cited by
- 11
- References
- 78
- Access
- Open access
- OpenAlex
- https://openalex.org/W15660380
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:12835559
Keywords
Art
References
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- Structures of the M2 channel-lining segments from nicotinic acetylcholine and NMDA receptors by NMR spectroscopy
- Structure and topology of a peptide segment of the 6th transmembrane domain of the Saccharomyces cerevisae alpha-factor receptor in phospholipid bilayers.
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- Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
- Elucidation of cross relaxation in liquids by two-dimensional N.M.R. spectroscopy
- Structure of segments of a G protein-coupled receptor: CD and NMR analysis of the Saccharomyces cerevisiae tridecapeptide pheromone receptor.
- Phosphorylation of T cell receptor ζ is regulated by a lipid dependent folding transition
- Clean TOCSY for proton spin system identification in macromolecules
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Cited by
- Physical interaction and functional coupling between ACDP4 and the intracellular ion chaperone COX11, an implication of the role of ACDP4 in essential metal ion transport and homeostasis
- Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters.
- Isolation, folding and structural investigations of the amino acid transporter OEP16.
- Structure and topology of Slc11a1(164-191) with G169D mutation in membrane-mimetic environments.
- Mutations in the gene encoding DMT1: clinical presentation and treatment.
- Structure analysis of the fourth transmembrane domain of Nramp1 in model membranes.
- Blood iron homeostasis: newly discovered proteins and iron imbalance.
- Structure, topology and assembly of a 32-mer peptide corresponding to the loop 3 and transmembrane domain 4 of divalent metal transporter (DMT1) in membrane-mimetic environments.
- T178 deletion impairs intermolecular interaction of the peptide Nramp1(164–191)
- HFIP-induced structures and assemblies of the peptides from the transmembrane domain 4 of membrane protein Nramp1.
- Alpha-helical transmembrane peptides: a "divide and conquer" approach to membrane proteins.
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