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

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JournalActa Crystallographica Section D: Biological Crystallography
DatePublished - 1 Nov 1998
Volume54
Number of pages4
Pages (from-to)1471-1474
Original languageEnglish

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.

    Research areas

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

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