Related ArticlesNMR spectroscopic studies of the DNA-binding domain of the monomer-binding nuclear orphan receptor, human estrogen related receptor-2. The carboxyl-terminal extension to the zinc-finger region is unstructured in the free form of the protein.
J Biol Chem. 1997 Jul 18;272(29):18038-43
Authors: Sem DS, Casimiro DR, Kliewer SA, Provencal J, Evans RM, Wright PE
Unlike steroid and retinoid receptors, which associate with DNA as dimers, human estrogen related receptor-2 (hERR2) belongs to a growing subclass of nuclear hormone receptors that bind DNA with high affinity as monomers. A carboxyl-terminal extension (CTE) to the zinc-finger domain has been implicated to be responsible for determining the stoichiometry of binding by a nuclear receptor to its response element. To better understand the mechanism by which DNA specificity is achieved, the solution structure of the DNA-binding domain of hERR2 (residues 96-194) consisting of the two putative zinc fingers and the requisite 26-amino acid CTE was analyzed by multidimensional heteronuclear magnetic resonance spectroscopy. The highly conserved zinc-finger region (residues 103-168) has a fold similar to those reported for steroid and retinoid receptors, with two helices that originate from the carboxyl-terminal ends of the two zinc fingers and that pack together orthogonally, forming a hydrophobic core. The CTE element of hERR2 is unstructured and highly flexible, exhibiting nearly random coil chemical shifts, extreme sensitivity of the backbone amide protons to solvent presaturation, and reduced heteronuclear (1H-15N) nuclear Overhauser effect values. This is in contrast to the dimer-binding retinoid X and thyroid hormone receptors, where, in each case, a helix has been observed within the CTE. The implications of this property of the hERR2 CTE are discussed.
[NMR paper] Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of mu
Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.
Related Articles Biochemical characterization and NMR studies of the nucleotide-binding domain 1 of multidrug-resistance-associated protein 1: evidence for interaction between ATP and Trp653.
Biochem J. 2003 Dec 15;376(Pt 3):749-56
Authors: Ramaen O, Masscheleyn S, Duffieux F, Pamlard O, Oberkampf M, Lallemand JY, Stoven V, Jacquet E
Multidrug-resistance-associated...
nmrlearner
Journal club
0
11-24-2010 09:16 PM
[NMR paper] NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM pr
NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Related Articles NMR and ICP spectroscopic analysis of the DNA-binding domain of the Drosophila GCM protein reveals a novel Zn2+ -binding motif.
Protein Eng. 2003 Apr;16(4):247-54
Authors: Shimizu M, Hiroaki H, Kohda D, Hosoya T, Akiyama-Oda Y, Hotta Y, Morita EH, Morikawa K
Drosophila GCM (glial cell missing) is a novel DNA-binding protein that determines the fate of glial precursors from the neural default to glia....
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[NMR paper] 111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein
111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 111Cd NMR studies of the domain specificity of Ag+ and Cu+ binding to metallothionein.
Biochemistry. 1996 Nov 5;35(44):13929-36
Authors: Li H, Otvos JD
Metal displacement reactions of Cd7MT with Ag+ or Cu+ and interprotein metal exchange reactions between Cd7MT and Ag12MT or Cu12MT were studied by 111Cd NMR. Titration of 111Cd7MT with Ag+ indicates that...
nmrlearner
Journal club
0
08-22-2010 02:20 PM
[NMR paper] MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domai
MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain.
Related Articles MCD, EPR and NMR spectroscopic studies of rabbit hemopexin and its heme binding domain.
Biochim Biophys Acta. 1995 Dec 6;1253(2):215-23
Authors: Cox MC, Le Brun N, Thomson AJ, Smith A, Morgan WT, Moore GR
Heme binding to rabbit hemopexin and its domain I, obtained by proteolytic cleavage of intact hemopexin, was studied by EPR, MCD and 1H-NMR spectroscopies. The data obtained support the proposal that the heme Fe(III) is coordinated by two...
nmrlearner
Journal club
0
08-22-2010 03:50 AM
[NMR paper] NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N as
NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure.
Related Articles NMR studies of the POU-specific DNA-binding domain of Oct-1: sequential 1H and 15N assignments and secondary structure.
Biochemistry. 1993 Jun 15;32(23):6032-40
Authors: Cox M, Dekker N, Boelens R, Verrijzer CP, van der Vliet PC, Kaptein R
The 1H and 15N resonances of the POU-specific DNA-binding domain of transcription factor Oct-1 have been assigned sequentially using two-dimensional homo- and heteronuclear...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid rec
Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor.
Related Articles Cadmium-113 NMR studies of the DNA binding domain of the mammalian glucocorticoid receptor.
Biochemistry. 1990 Oct 2;29(39):9218-25
Authors: Pan T, Freedman LP, Coleman JE
The DNA binding domain of the mammalian glucocorticoid hormone receptor (GR) contains nine highly conserved cysteine residues, a conservation shared by the superfamily of steroid and thyroid hormone receptors. A fragment consisting of GR residues 407-556, containing...
nmrlearner
Journal club
0
08-21-2010 11:04 PM
[NMR paper] NMR structure and functional studies of the Mu repressor DNA-binding domain.
NMR structure and functional studies of the Mu repressor DNA-binding domain.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR structure and functional studies of the Mu repressor DNA-binding domain.
Biochemistry. 1999 Jun 29;38(26):8367-76
Authors: Ilangovan U, Wojciak JM, Connolly KM, Clubb RT
The repressor protein of bacteriophage Mu establishes and maintains lysogeny by shutting down transposition functions needed for phage DNA replication. It interacts with several repeated DNA...