1f9f
From Proteopedia
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| - | [[Image:1f9f.gif|left|200px]] | + | [[Image:1f9f.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAIN''' | + | {{Structure |
| + | |PDB= 1f9f |SIZE=350|CAPTION= <scene name='initialview01'>1f9f</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE HPV-18 E2 DNA-BINDING DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1F9F is a [ | + | 1F9F is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_papillomavirus_type_63 Human papillomavirus type 63]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F9F OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10906136 10906136] |
[[Category: Human papillomavirus type 63]] | [[Category: Human papillomavirus type 63]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: trans-acting factor]] | [[Category: trans-acting factor]] | ||
| - | ''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 11:06:12 2008'' |
Revision as of 09:06, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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