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Core domain interactions in full-length p53 in solution
The tumor suppressor p53 consists of four 393-residue chains, each of which has two natively unfolded (N- and C-terminal) and two folded (core and tetramerization) domains. Their structural organization is poorly characterized as the protein tends to aggregate, has defied crystallization, and is at...
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| Auteurs principaux: | , , , , , , , |
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| Format: | Artigo |
| Langue: | Inglês |
| Publié: |
National Academy of Sciences
2006
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| Sujets: | |
| Accès en ligne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC1413758/ https://ncbi.nlm.nih.gov/pubmed/16461914 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0511130103 |
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