Consequences of fuzziness in the NFκB/IκBα interaction.
Consequences of fuzziness in the NFκB/IκBα interaction.
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DOI：
10.1007/978-1-4614-0659-4_5
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发表时间：
2012
影响因子：
--
通讯作者：
Komives, Elizabeth A.
中科院分区：
文献类型：
--
作者：
Komives, Elizabeth A.
This chapter provides a short review of various biophysical experiments that have been applied to the inhibitor of kappa B, IκBα, and its binding partner, nuclear factor kappa B, or NF-κB. The picture that emerges from amide hydrogen/deuterium exchange, NMR, and binding kinetics experiments is one in which parts of both proteins are “fuzzy” in the free-state, and some parts remain “fuzzy” in the NF-κB•IκBα complex. The NF-κB family of transcription factors responds to inflammatory cytokines with rapid transcriptional activation, in which NF-κB enters the nucleus and binds DNA. Just as rapidly as transcription is activated, it is subsequently repressed by newly synthesized IkBa that also enters the nucleus and removes NF-κB from the DNA. Because IkBa is an ankyrin repeat protein, it’s “fuzziness” can be controlled by mutagenesis to stabilized the folded state. Experimental comparison with such stabilized mutants helps provide evidence that much of the system control depends on the “fuzziness” of IκBα.
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影响因子：
64.5
作者：
Huxford, T;Huang, DB;Ghosh, G
通讯作者：
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影响因子：
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作者：
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DOI：
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发表时间：
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影响因子：
11.1
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