(2013). ZF-CxxC domain-con- taining proteins, CpG islands and the chromatin connection. Biochem. Soc. Trans. 41, 727-740.Long HK, Blackledge NP, Klose RJ. ZF-CxxC domain-containing proteins, CpG islands and the chromatin connection . Biochem Soc Trans . 2013; 41 : 727–740...
CXXC domain proteins direct different chromatin-modifying activities to various chromatin regions. Here, we report crystal structures of the CFP1 CXXC domain in complex with six different CpG DNA sequences. The crescent-shaped CFP1 CXXC domain is wedged into the major groove of the CpG DNA, ...
TET1 and TET3 possess an N-terminal CXXC domain, corresponding to a binuclear Zn-chelating domain also found in other chromatin-associated proteins such as DNMT1, CFP1 and MBD1 [2, 6]. These CXXC domains can medi- ate interactions with multiple nuclear components including non-methylated CG...
Proteins that contain a CXXC motif within their DNA-binding domain, such as CXXC1, recognize CpG sequences and regulate gene expression.Proteins that contain a CXXC motif within their DNA-binding domain, such as CXXC1, recognize CpG sequences and regulate gene expression (Carlone and Skalnik,...
CXXC motif, a metal binding domain containing Cys-X-X-Cys motif, has been identified in various organisms. These proteins are capable of binding various types of heavy metals. In this study, heavy metal binding domain (CXXC motif) recombinant protein encoded from mcsA gene of S. aureus ...
Presumably, the Tet proteins also show functional differences, but their specific properties are currently not understood. The Tet1 and Tet3 5mC oxidases are characterized by two conserved domains, an N-terminal CXXC domain that binds to CpG dinucleotides and a C-terminal Fe(II)- and 2-...
Redox Potential Measurement—Proteins with redox potentials that were to be measured were incubated with the γ-domain of DsbD, a protein with a known redox potential of -235 mV (27). At equilibrium, different protein species were separated by reverse-phase HPLC,2 and the equilibrium constant ...
first reported that mammalian ALR is a FAD-linked sulfhydryl oxidase (SOX) with a CXXC active motif at residues 62–65 in the carboxy-terminal domain [5] that is capable of catalyzing disulfide bond formation in a number of proteins [6]. According to the crystallisation data [7], the ...
first reported that mammalian ALR is a FAD-linked sulfhydryl oxidase (SOX) with a CXXC active motif at residues 62–65 in the carboxy-terminal domain [5] that is capable of catalyzing disulfide bond formation in a number of proteins [6]. According to the crystallisation data [7], the ...
These resulting chimeric proteins act as transcriptional regulators that take control of MLL targets. MLL fuses with more than 60 different partner genes, these fusion proteins retain the CXXC domain which binds to nonmethylated CpG DNA. The Molecular docking of CXXC domain and CpG dinucleotides ...