1ilc
From Proteopedia
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DNA Bending by an Adenine-Thymine Tract and Its Role in Gene Regulation.
Overview
To gain insight into the structural basis of DNA bending by, adenine-thymine tracts (A-tracts) and their role in DNA recognition by, gene-regulatory proteins, we have determined the crystal structure of the, high-affinity DNA target of the cancer-associated human papillomavirus E2, protein. The three independent B-DNA molecules of the crystal structure, determined at 2.2-A resolution are examples of A-tract-containing helices, where the global direction and magnitude of curvature are in accord with, solution data, thereby providing insights, at the base pair level, into, the mechanism of DNA bending by such sequence motifs. A comparative, analysis of E2-DNA conformations with respect to other structural and, biochemical studies demonstrates that (i) the A-tract structure of the, core region, which is not contacted by the protein, is critical for the, formation of the high-affinity sequence-specific protein-DNA complex, and, (ii) differential binding affinity is regulated by the intrinsic structure, and deformability encoded in the base sequence of the DNA target.
About this Structure
1ILC is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
DNA bending by an adenine--thymine tract and its role in gene regulation., Hizver J, Rozenberg H, Frolow F, Rabinovich D, Shakked Z, Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8490-5. Epub 2001 Jul 3. PMID:11438706
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