Analogs of cyclic AMP that elicit the biochemically defined conformational change in catabolite gene activator protein (CAP) but do not stimulate binding to DNA.
By R. Ebright, S. L. Grice, Jon P. Miller, Joseph S. Krakow. 1985
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Citations in the corpus
- Structural Basis of Dual Specificity of Sinorhizobium meliloti Clr, a cAMP and cGMP Receptor Protein (2023, background): “coli CAP as well, albeit without stimulating DNA binding (25).”
- Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, methodology): “To understand why cGMP, a noneffector molecule, binds to CAP but does not stimulate DNA binding by CAP (14, 15), we used NMR to characterize the CAP-cGMP2 complex.”
- Two-State Allosteric Modeling Suggests Protein Equilibrium as an Integral Component for Cyclic AMP (cAMP) Specificity in the cAMP Receptor Protein of Escherichia coli (2008, result): “This apparent discrepancy indicates that protease sensitivity only partially correlates with the active DNA-binding conformation of CRP protein, as has been noted previously (8).”