Abstract:Euplotes octocarinatus centrin (EoCen) is a member of the EF-hand superfamily of calcium-binding proteins, which refer to nucleotide excision repair (NER).
“…The binding mode of protein and DNA is mainly through the hydrogen bond or its complementary spatial structure with DNA structure or DNA special base sequence combination. 54 Fig. 4D is the overall superposition model structure of the interaction between HsCen2 and HsCen2p with DNA using ZDOCK 3.0.2.…”
Section: Resultsmentioning
confidence: 99%
“…The binding mode of protein and DNA is mainly through the hydrogen bond or its complementary spatial structure with DNA structure or DNA special base sequence combination. 54 is the overall superposition model structure of the interaction between HsCen2 and HsCen2p with DNA using ZDOCK 3.0.2. Structurally, the interaction between HsCen2 and DNA (cartoon: yellowish-brown) is such that the phosphate skeleton of DNA is stuck in the cavity formed between the EF3 and EF4 domains of HsCen2, and Ser170 in the C-terminal of HsCen2 is close to the base pair of the DNA.…”
Phosphorylation weakened the binding of Tb3+ to HsCen2, enhanced the binding of DNA to HsCen2; and improves the endonuclease-like activity of HsCen2; Additionally, the endonuclease-like activity of HsCen2 or HsCen2p is regulated up by Tb3+-binding.
“…The binding mode of protein and DNA is mainly through the hydrogen bond or its complementary spatial structure with DNA structure or DNA special base sequence combination. 54 Fig. 4D is the overall superposition model structure of the interaction between HsCen2 and HsCen2p with DNA using ZDOCK 3.0.2.…”
Section: Resultsmentioning
confidence: 99%
“…The binding mode of protein and DNA is mainly through the hydrogen bond or its complementary spatial structure with DNA structure or DNA special base sequence combination. 54 is the overall superposition model structure of the interaction between HsCen2 and HsCen2p with DNA using ZDOCK 3.0.2. Structurally, the interaction between HsCen2 and DNA (cartoon: yellowish-brown) is such that the phosphate skeleton of DNA is stuck in the cavity formed between the EF3 and EF4 domains of HsCen2, and Ser170 in the C-terminal of HsCen2 is close to the base pair of the DNA.…”
Phosphorylation weakened the binding of Tb3+ to HsCen2, enhanced the binding of DNA to HsCen2; and improves the endonuclease-like activity of HsCen2; Additionally, the endonuclease-like activity of HsCen2 or HsCen2p is regulated up by Tb3+-binding.
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