1ilc
From Proteopedia
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| - | [[Image:1ilc.gif|left|200px]] | + | [[Image:1ilc.gif|left|200px]] |
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| - | '''DNA Bending by an Adenine-Thymine Tract and Its Role in Gene Regulation.''' | + | {{Structure |
| + | |PDB= 1ilc |SIZE=350|CAPTION= <scene name='initialview01'>1ilc</scene>, resolution 2.2Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DNA Bending by an Adenine-Thymine Tract and Its Role in Gene Regulation.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1ILC is a [ | + | 1ILC is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ILC OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11438706 11438706] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Frolow, F.]] | [[Category: Frolow, F.]] | ||
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[[Category: hpv e2 dna target]] | [[Category: hpv e2 dna target]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:50 2008'' |
Revision as of 09:51, 20 March 2008
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| , resolution 2.2Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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