Related ArticlesSolution NMR structure of the C-terminal domain of the human protein DEK.
Protein Sci. 2004 Aug;13(8):2252-9
Authors: Devany M, Kotharu NP, Matsuo H
The chromatin-associated protein DEK was first identified as a fusion protein in patients with a subtype of acute myelogenous leukemia. It has since become associated with diverse human ailments ranging from cancers to autoimmune diseases. Despite much research effort, the biochemical basis for these clinical connections has yet to be explained. We have identified a structural domain in the C-terminal region of DEK [DEK(309-375)]. DEK(309-375) implies clinical importance because it can reverse the characteristic abnormal DNA-mutagen sensitivity in fibroblasts from ataxia-telangiectasia (A-T) patients. We determined the solution structure of DEK(309-375) by nuclear magnetic resonance spectroscopy, and found it to be structurally homologous to the E2F/DP transcription factor family. On the basis of this homology, we tested whether DEK(309-375) could bind DNA and identified the DNA-interacting surface. DEK presents a hydrophobic surface on the side opposite the DNA-interacting surface. The structure of the C-terminal region of DEK provides insights into the protein function of DEK.
[NMR paper] Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization
Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB.
Biochemistry. 2003 Feb 18;42(6):1460-9
Authors: Nguyen BD, Chen HT, Kobor MS, Greenblatt J, Legault P, Omichinski JG
FCP1 (TFIIF-associated CTD phosphatase) is the only known phosphatase specific for the phosphorylated CTD of RNAP II. The phosphatase activity of FCP1 is...
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[NMR paper] The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA bindi
The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
Related Articles The N-terminal domain of the human Rad51 protein binds DNA: structure and a DNA binding surface as revealed by NMR.
J Mol Biol. 1999 Jul 9;290(2):495-504
Authors: Aihara H, Ito Y, Kurumizaka H, Yokoyama S, Shibata T
Human Rad51 protein (HsRad51) is a homolog of Escherichia coli RecA protein, and functions in DNA repair and recombination. In higher eukaryotes, Rad51 protein is essential for cell viability. The...
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NMR solution structure of the N-terminal domain of hERG and its interaction with the
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
NMR solution structure of the N-terminal domain of hERG and its interaction with the S4-S5 linker.
Biochem Biophys Res Commun. 2010 Nov 2;
Authors: Li Q, Gayen S, Chen AS, Huang Q, Raida M, Kang C
The human Ether-ŕ-go-go Related Gene (hERG) potassium channel mediates the rapid delayed rectifier current (IKr) in the cardiac action potential. Mutations in the 135 amino acid residue N-terminal domain (NTD) cause channel dysfunction or...
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
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[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
...
Solution NMR structure of the C-terminal domain of the human protein DEK.
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