Roles of hinge region, loops 3 and 4 in the activation of Escherichia coli cyclic AMP receptor protein
| Autor: | Ting Yu, Guangrong Wu, Zhengya Gao, Feng Li, Shaoning Yu, Yanrun Zhu |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Conformational change
Cyclic AMP Receptor Protein Macromolecular Substances Protein Conformation Amino Acid Motifs Allosteric regulation lac operon Calorimetry medicine.disease_cause Biochemistry Structural Biology Escherichia coli medicine Chymotrypsin Molecular Biology biology Chemistry Circular Dichroism Escherichia coli Proteins Temperature General Medicine Protein Structure Tertiary Cell biology Kinetics Spectrometry Fluorescence cAMP receptor protein Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization biology.protein CAMP binding CREB1 Dimerization Protein Binding Signal Transduction |
| Zdroj: | International Journal of Biological Macromolecules. 50:1-6 |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2011.08.016 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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