Related ArticlesNMR structure of the human Mediator MED25 ACID domain.
J Struct Biol. 2010 Oct 22;
Authors: Bontems F, Verger A, Dewitte F, Lens Z, Baert JL, Ferreira E, de Launoit Y, Sizun C, Guittet E, Villeret V, Monté D
MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts with VP16 through a central MED25 PTOV (Prostate tumour overexpressed)/ACID (Activator interacting domain) domain of unknown structure. As a first step towards understanding the mechanism of recruitment of transactivation domains by MED25, we report here the NMR structure of the MED25 ACID domain. The domain architecture consists of a closed ?-barrel with seven strands (B1-B7) and three ?-helices (H1-H3), an architecture showing similarities to that of the SPOC (Spen paralog and ortholog C-terminal domain) domain-like superfamily. Preliminary NMR chemical shift mapping showed that VP16 H2 (VP16C) interacts with MED25 ACID through one face of the ?-barrel, defined by strands B4-B7-B6.
PMID: 20974256 [PubMed - as supplied by publisher]
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.
J Struct Funct Genomics. 2011 Jul 23;
Authors: Eletsky A, Ruyechan WT, Xiao R, Acton TB, Montelione GT, Szyperski T
The solution NMR structure of protein MED25(391-543), comprising the activator interacting domain (ACID) of subunit 25 of the human mediator, is presented along with the measurement of...
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[NMR paper] Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a muta
Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.
Related Articles Solution NMR structure of the SH3 domain of human nephrocystin and analysis of a mutation-causing juvenile nephronophthisis.
Proteins. 2005 May 1;59(2):347-55
Authors: le Maire A, Weber T, Saunier S, Broutin I, Antignac C, Ducruix A, Dardel F
Human nephrocystin is a protein associated with juvenile NPH, an autosomal recessive, inherited kidney disease responsible for chronic renal failure in children. It...
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[NMR paper] Solution NMR structure of the C-terminal domain of the human protein DEK.
Solution NMR structure of the C-terminal domain of the human protein DEK.
Related Articles Solution 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...
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[NMR paper] NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinas
NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding.
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J Biol Chem. 2003 Jul 11;278(28):25982-9
Authors: Liepinsh E, Banyai L, Pintacuda G, Trexler M, Patthy L, Otting G
...
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[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli
NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
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Biochemistry. 1998 Sep 15;37(37):12727-36
Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H
The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...
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[NMR paper] Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of
Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
Biochemistry. 1997 Feb 25;36(8):2132-8
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[NMR paper] Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of
Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm.
Biochemistry. 1997 Feb 25;36(8):2132-8
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[NMR paper] The structure of the human retinoic acid receptor-beta DNA-binding domain determined
The structure of the human retinoic acid receptor-beta DNA-binding domain determined by NMR.
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Nucleic Acids Symp Ser. 1992;(27):65-6
Authors: Katahira M, Knegtel R, Schilthius J, Boelens R, Eib D, van der Saag P, Kaptein R
The solution structure of the DNA-binding domain (DBD) of the human retinoic acid receptor-beta (hRAR-beta) has been determined by nuclear magnetic resonance (NMR) spectroscopy and distance geometry (DG). The...