1f9f
From Proteopedia
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CRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAIN
Overview
The papillomavirus E2 proteins regulate the transcription of all, papillomavirus genes and are necessary for viral DNA replication., Disruption of the E2 gene is commonly associated with malignancy in, cervical carcinoma, indicating that E2 has a role in regulating tumor, progression. Although the E2 proteins from all characterized, papillomaviruses bind specifically to the same 12-base pair DNA sequence, the cancer-associated human papillomavirus E2 proteins display a unique, ability to detect DNA flexibility and intrinsic curvature. To understand, the structural basis for this phenomenon, we have determined the crystal, structures of the human papillomavirus-18 E2 DNA-binding domain and its, complexes with high and low affinity binding sites. The E2 protein is a, dimeric beta-barrel and the E2-DNA interaction is accompanied by a large, deformation of the DNA as it conforms to the E2 surface. DNA conformation, and E2-DNA contacts are similar in both high and low affinity complexes., The differences in affinity correlate with the flexibility of the DNA, sequence. Preferences of E2 proteins from different papillomavirus strains, for flexible or prevent DNA targets correlate with the distribution of, positive charge on their DNA interaction surfaces, suggesting a role for, electrostatic forces in the recognition of DNA deformability.
About this Structure
1F9F is a Single protein structure of sequence from Human papillomavirus type 63 with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
The structural basis of DNA target discrimination by papillomavirus E2 proteins., Kim SS, Tam JK, Wang AF, Hegde RS, J Biol Chem. 2000 Oct 6;275(40):31245-54. PMID:10906136
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