Publications by authors named "Malka Kitayner"
p53 binds as a tetramer to DNA targets consisting of two decameric half-sites separated by a variable spacer. Here we present high-resolution crystal structures of complexes between p53 core-domain tetramers and DNA targets consisting of contiguous half-sites. In contrast to previously reported p53-DNA complexes that show standard Watson-Crick base pairs, the newly reported structures show noncanonical Hoogsteen base-pairing geometry at the central A-T doublet of each half-site.
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- The protein p53 plays a crucial role in preventing cancer by activating genes that stop the cell cycle or trigger cell death in response to stress.
- High-resolution crystal structures reveal that p53 forms a tetramer by binding to specific DNA half-sites, with interactions stabilized by protein-protein and base-stacking contacts.
- The study provides insights into how p53's DNA binding varies with different base sequences, enhancing our understanding of its specificity and regulatory mechanisms.
Structures of the DNA-binding site of Runt-domain transcription regulators.
Acta Crystallogr D Biol Crystallogr
March 2005
Runt-domain (RD) proteins are transcription factors that play fundamental roles in various developmental pathways. They bind specifically to DNA sequences of the general form PyGPyGGTPy (Py = pyrimidine), through which they regulate transcription of target genes. The DNA duplex TCTGCGGTC/TGACCGCAG, incorporating the binding site for the RD transcription factors (bold), was crystallized in space group P4(3).
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