Expression, crystallization and preliminary X-ray analysis of the E2 transactivation domain from papillomavirus type 16

J E  Burns; O V  Moroz; A A  Antson; C M  Sanders; K S  Wilson; N J  Maitland

Expression, crystallization and preliminary X-ray analysis of the E2 transactivation domain from papillomavirus type 16

J E Burns, O V Moroz, A A Antson, C M Sanders, K S Wilson, N J Maitland

Research output: Contribution to journal › Article › peer-review

Abstract

The N-terminal transactivation domain of the E2 protein from human papillomavirus type 16 has been crystallized by vapour diffusion. Crystals belong to the space group P3(1)21 (or P3(2)21) with unit-cell dimensions a = b = 54.3, c = 155.5 Angstrom. There is one molecule per asymmetric unit with a solvent content of 55%. Crystals diffract to at least 2.5 Angstrom resolution and complete X-ray data to 3.4 Angstrom have been collected on a conventional laboratory source. This 201-amino-acid domain of the E2 protein has been shown to interact functionally with both the HPV E1 protein and at least three cellular transcription factors, to fulfil its role in the control of viral transcription and replication. A knowledge of the structural basis of these multiple interactions should lead to a fuller understanding of the mechanism of action of this key regulator of the HPV life cycle.

Original language	English
Pages (from-to)	1471-1474
Number of pages	4
Journal	Acta Crystallographica. Section D, Biological Crystallography
Volume	54
Publication status	Published - 1 Nov 1998

Keywords

TRANSCRIPTION FACTORS
TRANS-ACTIVATION
E1 PROTEIN
BINDING
DNA
GENE
KERATINOCYTES
REGION

Cite this

@article{72a8b55e174e411096e4f8bb42385dc3,

title = "Expression, crystallization and preliminary X-ray analysis of the E2 transactivation domain from papillomavirus type 16",

abstract = "The N-terminal transactivation domain of the E2 protein from human papillomavirus type 16 has been crystallized by vapour diffusion. Crystals belong to the space group P3(1)21 (or P3(2)21) with unit-cell dimensions a = b = 54.3, c = 155.5 Angstrom. There is one molecule per asymmetric unit with a solvent content of 55%. Crystals diffract to at least 2.5 Angstrom resolution and complete X-ray data to 3.4 Angstrom have been collected on a conventional laboratory source. This 201-amino-acid domain of the E2 protein has been shown to interact functionally with both the HPV E1 protein and at least three cellular transcription factors, to fulfil its role in the control of viral transcription and replication. A knowledge of the structural basis of these multiple interactions should lead to a fuller understanding of the mechanism of action of this key regulator of the HPV life cycle.",

keywords = "TRANSCRIPTION FACTORS, TRANS-ACTIVATION, E1 PROTEIN, BINDING, DNA, GENE, KERATINOCYTES, REGION",

author = "Burns, {J E} and Moroz, {O V} and Antson, {A A} and Sanders, {C M} and Wilson, {K S} and Maitland, {N J}",

year = "1998",

month = nov,

day = "1",

language = "English",

volume = "54",

pages = "1471--1474",

journal = "Acta Crystallographica. Section D, Biological Crystallography",

issn = "0907-4449",

publisher = "International Union of Crystallography",

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TY - JOUR

T1 - Expression, crystallization and preliminary X-ray analysis of the E2 transactivation domain from papillomavirus type 16

AU - Burns, J E

AU - Moroz, O V

AU - Antson, A A

AU - Sanders, C M

AU - Wilson, K S

AU - Maitland, N J

PY - 1998/11/1

Y1 - 1998/11/1

N2 - The N-terminal transactivation domain of the E2 protein from human papillomavirus type 16 has been crystallized by vapour diffusion. Crystals belong to the space group P3(1)21 (or P3(2)21) with unit-cell dimensions a = b = 54.3, c = 155.5 Angstrom. There is one molecule per asymmetric unit with a solvent content of 55%. Crystals diffract to at least 2.5 Angstrom resolution and complete X-ray data to 3.4 Angstrom have been collected on a conventional laboratory source. This 201-amino-acid domain of the E2 protein has been shown to interact functionally with both the HPV E1 protein and at least three cellular transcription factors, to fulfil its role in the control of viral transcription and replication. A knowledge of the structural basis of these multiple interactions should lead to a fuller understanding of the mechanism of action of this key regulator of the HPV life cycle.

AB - The N-terminal transactivation domain of the E2 protein from human papillomavirus type 16 has been crystallized by vapour diffusion. Crystals belong to the space group P3(1)21 (or P3(2)21) with unit-cell dimensions a = b = 54.3, c = 155.5 Angstrom. There is one molecule per asymmetric unit with a solvent content of 55%. Crystals diffract to at least 2.5 Angstrom resolution and complete X-ray data to 3.4 Angstrom have been collected on a conventional laboratory source. This 201-amino-acid domain of the E2 protein has been shown to interact functionally with both the HPV E1 protein and at least three cellular transcription factors, to fulfil its role in the control of viral transcription and replication. A knowledge of the structural basis of these multiple interactions should lead to a fuller understanding of the mechanism of action of this key regulator of the HPV life cycle.

KW - TRANSCRIPTION FACTORS

KW - TRANS-ACTIVATION

KW - E1 PROTEIN

KW - BINDING

KW - DNA

KW - GENE

KW - KERATINOCYTES

KW - REGION

M3 - Article

SN - 0907-4449

VL - 54

SP - 1471

EP - 1474

JO - Acta Crystallographica. Section D, Biological Crystallography

JF - Acta Crystallographica. Section D, Biological Crystallography

ER -