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Structural effects of mutations to the conserved salt-bridge in Crp4. Comparison of the structures of Crp4 (a), (E15D)-Crp4 (b), (E15G)-Crp4 (c) and (R7G)-Crp4 (d). While the overall fold of the peptide is retained structural changes are seen in the side chains around the point of mutation in the Crp4 analogues. The structure of (E15G)-appears to be most affected and changes to the backbone seems to be translated from the residue 10-15 loop down through the β-strand to residues 20-24.
