Related ArticlesNMR studies of a new family of DNA binding proteins: the THAP proteins.
J Biomol NMR. 2013 Jan 11;
Authors: Gervais V, Campagne S, Durand J, Muller I, Milon A
Abstract
The THAP (THanatos-Associated Protein) domain is an evolutionary conserved C2CH zinc-coordinating domain shared with a large family of cellular factors (THAP proteins). Many members of the THAP family act as transcription factors that control cell proliferation, cell cycle progression, angiogenesis, apoptosis and epigenetic gene silencing. They recognize specific DNA sequences in the promoters of target genes and subsequently recruit effector proteins. Recent structural and functional studies have allowed getting better insight into the nuclear and cellular functions of some THAP members and the molecular mechanisms by which they recognize DNA. The present article reviews recent advances in the knowledge of the THAP domains structures and their interaction with DNA, with a particular focus on NMR. It provides the solution structure of the THAP domain of THAP11, a recently characterized human THAP protein with important functions in transcription and cell growth in colon cancer.
PMID: 23306615 [PubMed - as supplied by publisher]
[NMR paper] Solution Structure, Dynamics and Binding Studies of a Family 11 Carbohydrate-Binding Module from Clostridium thermocellum (CtCBM11).
Solution Structure, Dynamics and Binding Studies of a Family 11 Carbohydrate-Binding Module from Clostridium thermocellum (CtCBM11).
Related Articles Solution Structure, Dynamics and Binding Studies of a Family 11 Carbohydrate-Binding Module from Clostridium thermocellum (CtCBM11).
Biochem J. 2013 Jan 29;
Authors: Viegas A, Sardinha J, Freire F, Duarte DF, Carvalho AL, Fontes CM, Romão MJ, Macedo AL, Cabrita EJ
Abstract
Non-catalytic cellulosomal carbohydrate-binding modules (CBMs) are responsible for increasing the catalytic efficiency of...
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02-03-2013 10:19 AM
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly.
J Struct Funct Genomics. 2011 Sep 9;
Authors: Yang Y, Ramelot TA, Cort JR, Wang H, Ciccosanti C, Jiang M, Janjua H, Acton TB, Xiao R, Everett JK, Montelione GT, Kennedy MA
Abstract
...
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09-10-2011 06:51 PM
Engineering [Ln(DPA)3]3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Engineering 3â?? binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions
Abstract Paramagnetic relaxation enhancements from unpaired electrons observed in nuclear magnetic resonance (NMR) spectra present powerful long-range distance restraints. The most frequently used paramagnetic tags, however, are tethered to the protein via disulfide bonds, requiring proteins with single cysteine residues for covalent attachment. Here we present a straightforward strategy to tag proteins site-specifically with paramagnetic lanthanides without a tether and...
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07-26-2011 11:11 AM
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
Interaction of a putative BH3 domain of clusterin with anti-apoptotic Bcl-2 family proteins as revealed by NMR spectroscopy.
Biochem Biophys Res Commun. 2011 Apr 19;
Authors: Lee DH, Ha JH, Kim Y, Bae KH, Park JY, Choi WS, Yoon HS, Park SG, Park BC, Yi GS, Chi SW
Clusterin (CLU) is a multifunctional glycoprotein that is overexpressed in prostate and breast cancers. Although CLU is known to be involved in the regulation...
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04-30-2011 12:36 PM
[NMR paper] 19F-NMR studies of retinol transfer between cellular retinol binding proteins and pho
19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
FEBS Lett. 1997 Feb 3;402(2-3):116-20
Authors: Rong D, Lin CL, d'Avignon DA, Lovey AJ, Rosenberger M, Li E
The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol...
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08-22-2010 03:31 PM
[NMR paper] 19F-NMR studies of retinol transfer between cellular retinol binding proteins and pho
19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
FEBS Lett. 1997 Feb 3;402(2-3):116-20
Authors: Rong D, Lin CL, d'Avignon DA, Lovey AJ, Rosenberger M, Li E
The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol...
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08-22-2010 03:03 PM
[NMR paper] NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies
NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles NMR analysis of site-specific ligand binding in oligomeric proteins. Dynamic studies on the interaction of riboflavin synthase with trifluoromethyl-substituted intermediates.
Biochemistry. 1996 Jul 30;35(30):9637-46
Authors: Scheuring J, Fischer M, Cushman M, Lee J, Bacher A,...
NMR studies of a new family of DNA binding proteins: the THAP proteins.
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