Related ArticlesNMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Biochemistry. 1994 Jan 11;33(1):10-6
Authors: Vuister GW, Kim SJ, Wu C, Bax A
Heteronuclear multidimensional NMR experiments of residues 33-163 of the DNA-binding domain of Drosophila heat shock factor, dHSF(33-163), were recorded, using only 3 mg of uniformly 15N-labeled or 2 mg of uniformly 15N/13C-labeled protein. The polypeptide consists of a structured part comprising three helices, a three-stranded antiparallel beta-sheet, with the first two strands connected by a four-residue type I tight turn. The second helix is disrupted at its C-terminal end by a proline residue and is followed by an extended turn, leading to the third helix. The dHSF(33-163) protein is unstructured at its N- and C-termini, and a third unstructured region is found from Thr113 to Arg124. Exchange broadening of the 15N-1H correlations upon titration of 15N labeled HSF with a 13-base-pair DNA duplex suggests a DNA-binding motif in which the third helix acts as the recognition helix. Both the secondary structure and DNA-binding pattern of dHSF(33-163) suggest that the overall topology resembles that the helix-turn-helix bacterial activator CAP [Weber, I. T., & Steitz, T. A. (1987) J. Mol. Biol. 198, 311-326] and the liver-specific transcription factor HNF-3 gamma, the prototype of the HNF-3/forkhead protein family [Clark, K. L., Halay, E. D., Lai, E., & Burley, S. K. (1993) Nature 364, 412-420].
Searching the protein structure database for ligand-binding site similarities ... - 7thSpace Interactive (press release)
Searching the protein structure database for ligand-binding site similarities ... - 7thSpace Interactive (press release)
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Searching the protein structure database for ligand-binding site similarities ...
7thSpace Interactive (press release)
CPASS is an important component of our Functional Annotation Screening Technology by NMR (FAST-NMR) protocol and has been successfully applied to aid the ...
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[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.
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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....
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[NMR paper] Mapping the interacting regions between troponins T and C. Binding of TnT and TnI pep
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J Biol Chem. 2001 Sep 28;276(39):36606-12
Authors: Blumenschein TM, Tripet BP, Hodges RS, Sykes BD
Muscular contraction is triggered by an increase in calcium concentration, which is transmitted to the contractile proteins by the troponin...
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Evaluation of protein adsorption and preferred binding regions in multimodal chromato
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Proc Natl Acad Sci U S A. 2010 Sep 13;
Authors: Chung WK, Freed AS, Holstein MA, McCallum SA, Cramer SM
NMR titration experiments with labeled human ubiquitin were employed in concert with chromatographic data obtained with a library of ubiquitin mutants to study the nature of protein adsorption in multimodal (MM) chromatography....
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[NMR paper] NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reve
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EMBO J. 1995 Jul 17;14(14):3563-71
Authors: Bycroft M, GrĂ¼nert S, Murzin AG, Proctor M, St Johnston D
The...
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[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
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J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...
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[NMR paper] NMR evidence for similarities between the DNA-binding regions of Drosophila melanogas
NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Related Articles NMR evidence for similarities between the DNA-binding regions of Drosophila melanogaster heat shock factor and the helix-turn-helix and HNF-3/forkhead families of transcription factors.
Biochemistry. 1994 Jan 11;33(1):10-6
Authors: Vuister GW, Kim SJ, Wu C, Bax A
Heteronuclear multidimensional NMR experiments of residues 33-163 of the...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] NMR studies of peptides derived from the putative binding regions of cartilage protei
NMR studies of peptides derived from the putative binding regions of cartilage proteins. No evidence for binding to hyaluronan.
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J Biol Chem. 1994 Jan 21;269(3):1699-704
Authors: Horita DA, Hajduk PJ, Goetinck PF, Lerner LE
Previous work has implicated sequences within the tandem repeats of cartilage link protein in the interaction of link protein with hyaluronan. This conclusion was based on...