Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees
By S. Schultz, G. Shields, T. Steitz. 1991
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Citations in the corpus
- 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, background): “The cAMP specificity of wild-type (WT) CRP is consistent with the structure of active CRP, which has been characterized a number of times and shows specific contacts between protein residues and cAMP (27, 29, 33).”
- DNA Deformation Energy as an Indirect Recognition Mechanism in Protein-DNA Interactions (2007, background): “All sequences known to bind to IHF [23], CRP [19], [20], I-CreI [21] , I-PpoI [21], and SRF [22] at high affinities were identified from the available literature (see supplemental data).”
- An overview of the structures of protein-DNA complexes (2000, unknown): “A2(103-160), B1(5-75), B2(102-161) 1oct C1(5-75) Oct-1 POU domain H.”
- Structural basis for cAMP-mediated allosteric control of the catabolite activator protein (2009, background): “The 3D structures of CAP have been determined in its cAMP-bound state (6) and in its cAMP-bound state in complex with DNA (7, 8).”