Structure analysis of the fourth transmembrane domain of Nramp1 in model membranes.
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Summary
It is found that an alpha-helix is predominantly induced in membrane-mimetic environments and the folding of the C-terminal residues is regulated by pH in SDS micelles, and the self-association of the peptide is also observed in TFE.
- Type
- article
- Published
- 2008-06-01
- Cited by
- 14
- References
- 65
- OpenAlex
- https://openalex.org/W2010869016
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24843384
Keywords
Micelle, Transmembrane domain, Peptide, Chemistry, Transmembrane protein
References
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- NMR structures and orientation of the fourth transmembrane domain of the rat divalent metal transporter (DMT1) with G185D mutation in SDS micelles
- The G185R mutation disrupts function of the iron transporter Nramp2.
- The role of interhelical ionic interactions in controlling protein folding and stability. De novo designed synthetic two-stranded alpha-helical coiled-coils.
- Cloning and characterization of a mammalian proton-coupled metal-ion transporter
- Recent progress in structure-function analyses of Nramp proton-dependent metal-ion transporters.
- pKA values of carboxyl groups in the native and denatured states of barnase: the pKA values of the denatured state are on average 0.4 units lower than those of model compounds.
- Electrostatic interactions in ubiquitin: stabilization of carboxylates by lysine amino groups.
- Divalent cation transport and susceptibility to infectious and autoimmune disease: continuation of the Ity/Lsh/Bcg/Nramp1/Slc11a1 gene story.
- NMR determination of pKa values for Asp, Glu, His, and Lys mutants at each variable contiguous enzyme-inhibitor contact position of the turkey ovomucoid third domain.
- The first external loop of the metal ion transporter DCT1 is involved in metal ion binding and specificity
- Characterization of the iron transporter DMT1 (NRAMP2/DCT1) in red blood cells of normal and anemic mk/mk mice.
- Genetic regulation of macrophage activation: understanding the function of Nramp1 (=Ity/Lsh/Bcg).
- Iron transporter Nramp2/DMT-1 is associated with the membrane of phagosomes in macrophages and Sertoli cells.
- Iron, manganese, and cobalt transport by Nramp1 (Slc11a1) and Nramp2 (Slc11a2) expressed at the plasma membrane.
- Comparison of mammalian cell lines expressing distinct isoforms of divalent metal transporter 1 in a tetracycline-regulated fashion.
- MOLMOL: a program for display and analysis of macromolecular structures.
- Natural-resistance-associated macrophage protein 1 is an H+/bivalent cation antiporter.
- Secondary structure and position of the cell-penetrating peptide transportan in SDS micelles as determined by NMR.
- Incomplete glycosylation and defective intracellular targeting of mutant solute carrier family 11 member 1 (Slc11a1).
Cited by
- Nramp: from sequence to structure and mechanism of divalent metal import.
- Penetration of three transmembrane segments of Slc11a1 in lipid bilayers.
- Structure and topology of Slc11a1(164-191) with G169D mutation in membrane-mimetic environments.
- Structure and transmembrane topology of slc11a1 TMD1–5 in lipid membranes
- T178 deletion impairs intermolecular interaction of the peptide Nramp1(164–191)
- Alpha-helical transmembrane peptides: a "divide and conquer" approach to membrane proteins.
- Hyaluronic acid hydrogel loaded with genetically-engineered brain-derived neurotrophic factor as a neural cell carrier.
- Design of Embedded-Hybrid Antimicrobial Peptides with Enhanced Cell Selectivity and Anti-Biofilm Activity
- Folding determinants of disulfide bond forming protein B explored by solution nuclear magnetic resonance spectroscopy
- Insight into the structures of the second and fifth transmembrane domains of Slc11a1 in membrane mimics
- High Specific Selectivity and Membrane-Active Mechanism of Synthetic Cationic Hybrid Antimicrobial Peptides Based on the Peptide FV7
- Structure and positioning of three transmembrane segments from Slc11a1 in SDS micelles
- Biophysical studies of membrane transport proteins from Nramp/MntH family and their function
- Binding Affinity of Full − length and Extracellular Domains of Recombinant Human (Pro)renin Receptors to Human Renin When Expressed in the Fat Body and Hemolymph of Silkworm Larvae
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