Solution structure of the core NFATC1/DNA complex
Article Abstract:
Research was conducted to study the solution composition of the binary complex established between the minimal DNA recognition domain of the human nuclear factor of the activated T cell (NFATC) and an oligonucleotide duplex characterized by the interleukin-2 enhancer sequence. Site-directed mutation was utilized to determine an Escherichia coli overexpression system for NFATC. Results indicated that the gain of DNA-binding affinity can be determined on the basis of the nuclear magnetic resonance complex structure.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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The crystal structure of haeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine and rearranged base pairing
Article Abstract:
X-ray crystallation of bacterial DNA (cytosine-5)-methyltransferase HaeIII covalently linked to DNA reveals that the cytosine is flipped out of the DNA helix and inserted into the active site of the enzyme, and the bases are unstacked, resulting in the formation of 8 Angstrom gap in the DNA. This differs from bacterial DNA (cytosine-5)-methyltransferase M. Hhal, which flips the cytosine out of the helix without unbending the helix.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
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Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision
Article Abstract:
The DNA n-glycosylase base excision-repair proteins can locate and cleave damaged bases from DNA, as the first stage in restoring the genetic blueprint. The crystal structure of human 3-methyladenine DNA glycosylase complexed to a mechanism-based pyrrolidine inhibitor is reported. The structure provides a way of exposing a nucelotide for base excision, along with a network of residues that can catalyze in-line displacement.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
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