2nnu

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(New page: 200px<br /> <applet load="2nnu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nnu, resolution 1.59&Aring;" /> '''Crystal Structure o...)
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'''Crystal Structure of the Papillomavirus DNA Tethering Complex E2:Brd4'''<br />
'''Crystal Structure of the Papillomavirus DNA Tethering Complex E2:Brd4'''<br />
==Overview==
==Overview==
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Many DNA viruses that are latent in dividing cells are noncovalent, passengers on mitotic chromosomes and require specific viral-encoded and, cellular factors for this activity. The chromosomal protein Brd4 is, implicated in the hitchhiking of bovine papillomavirus-1 (BPV-1), and the, viral protein E2 binds to both plasmids and Brd4. Here, we present the, X-ray crystal structure of the carboxy-terminal domain of Brd4 in complex, with HPV-16 E2, and with this information have developed a Brd4-Tat fusion, protein that is efficiently taken up by different transformed cells, harboring HPV plasmids. In cells treated with these fusion proteins for, only 2 hr and arrested in metaphase, the HPV DNA, either HPV-16 or -31, is, displaced from mitotic chromosomes. Mutant Brd4 peptides are deficient in, ablating this association. We suggest that such peptides may lead to the, development of inhibitors of latency for many, if not all, papillomaviruses.
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Many DNA viruses that are latent in dividing cells are noncovalent passengers on mitotic chromosomes and require specific viral-encoded and cellular factors for this activity. The chromosomal protein Brd4 is implicated in the hitchhiking of bovine papillomavirus-1 (BPV-1), and the viral protein E2 binds to both plasmids and Brd4. Here, we present the X-ray crystal structure of the carboxy-terminal domain of Brd4 in complex with HPV-16 E2, and with this information have developed a Brd4-Tat fusion protein that is efficiently taken up by different transformed cells harboring HPV plasmids. In cells treated with these fusion proteins for only 2 hr and arrested in metaphase, the HPV DNA, either HPV-16 or -31, is displaced from mitotic chromosomes. Mutant Brd4 peptides are deficient in ablating this association. We suggest that such peptides may lead to the development of inhibitors of latency for many, if not all, papillomaviruses.
==About this Structure==
==About this Structure==
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2NNU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_papillomavirus_type_13 Human papillomavirus type 13]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NNU OCA].
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2NNU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_papillomavirus_type_13 Human papillomavirus type 13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNU OCA].
==Reference==
==Reference==
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[[Category: Human papillomavirus type 13]]
[[Category: Human papillomavirus type 13]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Abbate, E.A.]]
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[[Category: Abbate, E A.]]
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[[Category: Botchan, M.R.]]
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[[Category: Botchan, M R.]]
[[Category: Voitenleitner, C.]]
[[Category: Voitenleitner, C.]]
[[Category: amphipathic helix]]
[[Category: amphipathic helix]]
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[[Category: three helix bundle]]
[[Category: three helix bundle]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:00:16 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:08:54 2008''

Revision as of 16:08, 21 February 2008


2nnu, resolution 1.59Å

Drag the structure with the mouse to rotate

Crystal Structure of the Papillomavirus DNA Tethering Complex E2:Brd4

Overview

Many DNA viruses that are latent in dividing cells are noncovalent passengers on mitotic chromosomes and require specific viral-encoded and cellular factors for this activity. The chromosomal protein Brd4 is implicated in the hitchhiking of bovine papillomavirus-1 (BPV-1), and the viral protein E2 binds to both plasmids and Brd4. Here, we present the X-ray crystal structure of the carboxy-terminal domain of Brd4 in complex with HPV-16 E2, and with this information have developed a Brd4-Tat fusion protein that is efficiently taken up by different transformed cells harboring HPV plasmids. In cells treated with these fusion proteins for only 2 hr and arrested in metaphase, the HPV DNA, either HPV-16 or -31, is displaced from mitotic chromosomes. Mutant Brd4 peptides are deficient in ablating this association. We suggest that such peptides may lead to the development of inhibitors of latency for many, if not all, papillomaviruses.

About this Structure

2NNU is a Protein complex structure of sequences from Homo sapiens and Human papillomavirus type 13. Full crystallographic information is available from OCA.

Reference

Structure of the papillomavirus DNA-tethering complex E2:Brd4 and a peptide that ablates HPV chromosomal association., Abbate EA, Voitenleitner C, Botchan MR, Mol Cell. 2006 Dec 28;24(6):877-89. PMID:17189190

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