| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8334985 | International Journal of Biological Macromolecules | 2012 | 6 Pages |
Abstract
The cAMP receptor protein (CRP) requires cAMP for an allosteric change and regulates more than 150 genes in Escherichia coli. In this study, the modular half of cAMP receptor protein was used to investigate the allosteric signal transmission pathway induced by cAMP binding. The activation of CRP upon cAMP binding is indicated to be realignment of the two subunits within the CRP dimer. The interaction of loop 3 and Phe136 do not involve in signal transmission.
Keywords
PMSFCyclic nucleotide-gated ion channelsCNGCEpacpKaPAGETFAITCIPTGHTP3′,5′-cyclic adenosine monophosphatecAMPTrifluoroacetic acidpolyacrylamide gel electrophoresisConformational changeANSphenylmethylsulfonyl fluoridewild-typeExchange protein directly activated by cAMPCRPprotein kinase AcAMP receptor proteinIsothermal titration calorimetry
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Authors
Zhengya Gao, Feng Li, Guangrong Wu, Yanrun Zhu, Ting Yu, Shaoning Yu,