Allosteric regulation of the cAMP receptor protein.

@article{Harman2001AllostericRO,
  title={Allosteric regulation of the cAMP receptor protein.},
  author={James Harman},
  journal={Biochimica et biophysica acta},
  year={2001},
  volume={1547 1},
  pages={
          1-17
        }
}
The cyclic AMP receptor protein (CRP) of Escherichia coli is a dimer made up of identical subunits. Each CRP subunit contains a cyclic nucleotide binding pocket and the CRP dimer exhibits negative cooperativity in binding cAMP. In solutions containing cAMP, CRP undergoes sequential conformation changes from the inactive apo-form through the active CRP:(cAMP)(1) complex to the less active CRP:(cAMP)(2) complex depending on the cAMP concentration. Apo-CRP binds DNA with low affinity and no… CONTINUE READING
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