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As shown in Figure 5, the analyses for both Trp54 and Lys134 show high allosteric transmission to three of the four Ni(II)-binding residues (His101, His99, and Cys107) in square planar His3Cys sites, which are conserved among NikR homologs ( 28 Jones, M. D., Sydor, A. M., and Zamble, D. B. (2013) NikR: Mechanism and function in nickel homeostasis. in Metals in Cells (Scott, R. S., and Culotta, V. eds.), John Wiley & Sons. pp 277-287 ).
Abstract Quantifying chemical substituent contributions to ligand binding free energies is challenging due to non-additive effects. Protein allostery is a frequent cause of non-additivity, but the underlying allosteric mechanisms often remain elusive. Here, we propose a general NMR-based approach to elucidate such mechanisms and we apply it to the HCN4 ion channel, whose cAMP-binding domain is an archetypal conformational switch.
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