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Title 

Structural origin for the transcriptional activity of human p53

Authors 

Si Hyung LeeKyu Hwan ParkDo Hyung KimDong Ho ChoungJae Eun SukJun ChangYoung Chul SungKwan Yong ChoiKyou Hoon Han

Publisher 

Springer Verlag (Germany)

Issue Date 

2001

Citation 

Journal of Biochemistry and Molecular Biology, vol. 34, no. 1, pp. 73-79

Keywords 

mouse double minute 2nuclear magnetic resonancep53transcriptional activation domainUnstructured

Abstract 

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 positionally 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→22R,23S). Results show that the mutant has an identical overall structural topology as the native protein, to the extent that the amphipathic helix formed by the residues 18T-26L within the native p53 transactivating domain is preserved in the double mutant. Therefore, the lack of transcriptional activity in the double mutant should be ascribed to the disruption of the essential hydrophobic contacts between the p53 transactivation domain and target proteins due to the (22L,23W→22R,23S) mutation.

ISSN 

1225-8687

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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