Allosteric changes in the cAMP receptor protein of Escherichia coli: hinge reorientation.

The cAMP receptor protein (CRP) of Escherichia coli is a dimer of a two-domain subunit. It requires binding of cAMP for a conformational change in order to function as a site-specific DNA-binding protein that regulates gene activity. The hinge region connecting the cAMP-binding domain to the DNA-bin...

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Опубликовано в::	Proc Natl Acad Sci U S A
Главные авторы:	Kim, J, Adhya, S, Garges, S
Формат:	Artigo
Язык:	Inglês
Опубликовано:	National Academy of Sciences 1992
Предметы:	Research Article
Online-ссылка:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC50200/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1409686/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.89.20.9700
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