BMB Reports
- 제34권1호
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- Pages.73-79
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- 2001
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- 1976-670X(eISSN)
Structural Origin for the Transcriptional Activity of Human p53
- Lee, Si-Hyung (Protein Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
- Park, Kyu-Hwan (Protein Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
- Kim, Do-Hyung (Protein Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
- Choung, Dong-Ho (Protein Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
- Suk, Jae-Eun (Protein Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology) ;
- Kim, Do-Hyung (Department of Life Sciences, Center for Biofunctional Molecules and School of Environmental Engineering, Pohang University of Science and Technology) ;
- Chang, Jun (Department of Life Sciences, Center for Biofunctional Molecules and School of Environmental Engineering, Pohang University of Science and Technology) ;
- Sung, Young-Chul (Department of Life Sciences, Center for Biofunctional Molecules and School of Environmental Engineering, Pohang University of Science and Technology) ;
- Choi, Kwan-Yong (Department of Life Sciences, Center for Biofunctional Molecules and School of Environmental Engineering, Pohang University of Science and Technology) ;
- Han, Kyou-Hoon (Protein Engineering Laboratory, Korea Research Institute of Bioscience and Biotechnology)
- 투고 : 2000.11.01
- 심사 : 2000.12.18
- 발행 : 2001.01.31
초록
Transcriptional activation domains are known to be inherently "unstructured" with no tertiary structure. A recent NMR study, however, has shown that the transactivation domain in human p53 is populated with an amphipathic helix and two nascent turns. This suggests that the presence of such local secondary structures within the overall "unstructured" structural framework is a general feature of acidic transactivation domains. These pre-existing local structures in p53, formed selectively by positional conserved hydrophobic residues that are known to be critical for transcriptional activity, thus appear to constitute the specific structural motifs that regulate recognition of the p53 transactivation domain by target proteins. Here, we report the results of a NMR structural comparison between the native human p53 transactivation domain and an inactive mutant (22L,23W
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