1QQH
2.1 A CRYSTAL STRUCTURE OF THE HUMAN PAPILLOMAVIRUS TYPE 18 E2 ACTIVATION DOMAIN
Summary for 1QQH
| Entry DOI | 10.2210/pdb1qqh/pdb |
| Descriptor | PAPILLOMAVIRUS TRANSCRIPTION FACTOR E2 (2 entities in total) |
| Functional Keywords | amphipathic helix, cashew/kidney shape, viral protein |
| Biological source | Human papillomavirus type 18 |
| Cellular location | Host nucleus : P06790 |
| Total number of polymer chains | 1 |
| Total formula weight | 16481.14 |
| Authors | Harris, S.F.,Botchan, M.R. (deposition date: 1999-06-05, release date: 1999-06-21, Last modification date: 2024-02-14) |
| Primary citation | Harris, S.F.,Botchan, M.R. Crystal structure of the human papillomavirus type 18 E2 activation domain. Science, 284:1673-1677, 1999 Cited by PubMed Abstract: The papillomavirus E2 protein regulates viral transcription and DNA replication through interactions with cellular and viral proteins. The amino-terminal activation domain, which represents a protein class whose structural themes are poorly understood, contains key residues that mediate these functional contacts. The crystal structure of a protease-resistant core of the human papillomavirus type 18 E2 activation domain reveals a novel fold creating a cashew-shaped form with a glutamine-rich alpha helix packed against a beta-sheet framework. The protein surface shows extensive overlap of determinants for replication and transcription. The structure broadens the concept of activators to include proteins with potentially malleable, but certainly ordered, structures. PubMed: 10356398DOI: 10.1126/science.284.5420.1673 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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