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...
nmrlearner
Journal club
0
07-26-2011 09:30 PM
[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...
nmrlearner
Journal club
0
11-25-2010 08:21 PM
[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...
nmrlearner
Journal club
0
11-24-2010 09:51 PM
[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.
Related Articles 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.
J Biol Chem. 2003 Jul 11;278(28):25982-9
Authors: Liepinsh E, Banyai L, Pintacuda G, Trexler M, Patthy L, Otting G
...
nmrlearner
Journal club
0
11-24-2010 09:01 PM
[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.
Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
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...
nmrlearner
Journal club
0
11-17-2010 11:15 PM
[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
...
nmrlearner
Journal club
0
08-22-2010 03:31 PM
[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
...
nmrlearner
Journal club
0
08-22-2010 03:03 PM
[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.
Related Articles The structure of the human retinoic acid receptor-beta DNA-binding domain determined by NMR.
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...
NMR structure of the human Mediator MED25 ACID domain.
Linear Mode
