Title : Mapping conformational changes in a protein: application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein.

Pub. Date : 1997 Sep 9

PMID : 9283073






5 Functional Relationships(s)
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1 Mapping conformational changes in a protein: application of a protein footprinting technique to cAMP-induced conformational changes in cAMP receptor protein. Cyclic AMP C-reactive protein Homo sapiens
2 The binding of cAMP to CRP dramatically increases the specific DNA binding activity of the protein and, as has been previously shown, induces conformational changes in the protein. Cyclic AMP C-reactive protein Homo sapiens
3 Binding of cAMP produced measurable differences in the susceptibility of CRP to the cleavage by Fe-EDTA. Cyclic AMP C-reactive protein Homo sapiens
4 The F alpha-helix, which provides all base-specific contacts in the CRP-DNA complex, became hypersensitive to Fe-EDTA-mediated cleavage, whereas the solvent exposure of D and E alpha-helices was decreased upon binding of cAMP. Cyclic AMP C-reactive protein Homo sapiens
5 These results suggest that a significant part of cAMP-induced conformational change in CRP involves a movement of secondary structure elements in the C-terminal domain of the protein so that the recognition F alpha-helix becomes exposed to the solvent. Cyclic AMP C-reactive protein Homo sapiens