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The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding.
The p53 tumor suppressor forms stable tetramers, whose DNA binding activity is allosterically regulated. The tetramerization domain is contained within the C-terminus (residues 323-355) and its three-dimensional structure exhibits dihedral symmetry, such that a p53 tetramer can be considered a dimer...
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| Publicado no: | EMBO J |
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| Main Authors: | , , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
Nature Publishing Group
1995
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC398109/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/7859740/ https://ncbi.nlm.nih.govhttps://doi.org/10.1002/j.1460-2075.1995.tb07027.x |
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