1r8h
From Proteopedia
(New page: 200px<br /><applet load="1r8h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r8h, resolution 1.90Å" /> '''Comparison of the st...) |
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| - | [[Image:1r8h.gif|left|200px]]<br /><applet load="1r8h" size=" | + | [[Image:1r8h.gif|left|200px]]<br /><applet load="1r8h" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r8h, resolution 1.90Å" /> | caption="1r8h, resolution 1.90Å" /> | ||
'''Comparison of the structure and DNA binding properties of the E2 proteins from an oncogenic and a non-oncogenic human papillomavirus'''<br /> | '''Comparison of the structure and DNA binding properties of the E2 proteins from an oncogenic and a non-oncogenic human papillomavirus'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human papillomaviruses (HPVS) that infect the genital tract can be divided | + | Human papillomaviruses (HPVS) that infect the genital tract can be divided into two groups: high-risk HPV types, such as HPV 16 and HPV 18, are associated with cancer, low-risk HPV types, such as HPV 6, are associated with benign warts. In both high-risk and low-risk HPV types, the papillomavirus E2 protein binds to four sites within the viral long control region (LCR) and regulates viral gene expression. Here, we present the crystal structure of the minimal DNA-binding domain (DBD) from the HPV 6 E2 protein. We show that the HPV 6 E2 DBD is structurally more similar to the HPV 18 and bovine papillomavirus type 1 (BPV1) E2 proteins than it is to the HPV 16 E2 protein. Using gel retardation assays, we show that the hierarchy of E2 sites within the HPV 16 and HPV 6 LCRs are different. However, despite these differences in structure and site preference, both the HPV 16 and 6 E2 DBDs recognise an extended version of the consensus E2 binding site derived from studies of the BPV1 E2 protein. In both cases, the preferred binding site is 5'AACCGN(4)CGGTT3', where the additional flanking base-pairs are in bold and N(4) represents a four base-pair central spacer. Both of these HPV proteins bind preferentially to E2 sites that contain an A:T-rich central spacer. We show that the preference for an A:T-rich central spacer is due, at least in part, to the need to adopt a DNA conformation that facilitates protein contacts with the flanking base-pairs. |
==About this Structure== | ==About this Structure== | ||
| - | 1R8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_papillomavirus_type_1a Human papillomavirus type 1a] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1R8H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_papillomavirus_type_1a Human papillomavirus type 1a] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Human papillomavirus type 1a]] | [[Category: Human papillomavirus type 1a]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brady, R | + | [[Category: Brady, R L.]] |
[[Category: Dell, G.]] | [[Category: Dell, G.]] | ||
[[Category: Gaston, K.]] | [[Category: Gaston, K.]] | ||
[[Category: Parish, J.]] | [[Category: Parish, J.]] | ||
[[Category: Tranter, R.]] | [[Category: Tranter, R.]] | ||
| - | [[Category: Wilkinson, K | + | [[Category: Wilkinson, K W.]] |
[[Category: PO4]] | [[Category: PO4]] | ||
[[Category: anti-parallel beta-barrel]] | [[Category: anti-parallel beta-barrel]] | ||
[[Category: dna-binding domain]] | [[Category: dna-binding domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:48:12 2008'' |
Revision as of 12:48, 21 February 2008
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Comparison of the structure and DNA binding properties of the E2 proteins from an oncogenic and a non-oncogenic human papillomavirus
Overview
Human papillomaviruses (HPVS) that infect the genital tract can be divided into two groups: high-risk HPV types, such as HPV 16 and HPV 18, are associated with cancer, low-risk HPV types, such as HPV 6, are associated with benign warts. In both high-risk and low-risk HPV types, the papillomavirus E2 protein binds to four sites within the viral long control region (LCR) and regulates viral gene expression. Here, we present the crystal structure of the minimal DNA-binding domain (DBD) from the HPV 6 E2 protein. We show that the HPV 6 E2 DBD is structurally more similar to the HPV 18 and bovine papillomavirus type 1 (BPV1) E2 proteins than it is to the HPV 16 E2 protein. Using gel retardation assays, we show that the hierarchy of E2 sites within the HPV 16 and HPV 6 LCRs are different. However, despite these differences in structure and site preference, both the HPV 16 and 6 E2 DBDs recognise an extended version of the consensus E2 binding site derived from studies of the BPV1 E2 protein. In both cases, the preferred binding site is 5'AACCGN(4)CGGTT3', where the additional flanking base-pairs are in bold and N(4) represents a four base-pair central spacer. Both of these HPV proteins bind preferentially to E2 sites that contain an A:T-rich central spacer. We show that the preference for an A:T-rich central spacer is due, at least in part, to the need to adopt a DNA conformation that facilitates protein contacts with the flanking base-pairs.
About this Structure
1R8H is a Single protein structure of sequence from Human papillomavirus type 1a with as ligand. Full crystallographic information is available from OCA.
Reference
Comparison of the structure and DNA-binding properties of the E2 proteins from an oncogenic and a non-oncogenic human papillomavirus., Dell G, Wilkinson KW, Tranter R, Parish J, Leo Brady R, Gaston K, J Mol Biol. 2003 Dec 12;334(5):979-91. PMID:14643661
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