Substrates Modulate Charge-Reorganization Allosteric Effects in Protein-Protein Association

Shirsendu Ghosh, Koyel Banerjee-ghosh, Dorit Levy, Inbal Riven, Ron Naaman, Gilad Haran

Research output: Contribution to journalArticlepeer-review


Protein function may be modulated by an event occurring far away from the functional site, a phenomenon termed allostery. While classically allostery involves conformational changes, we recently observed that charge redistribution within an antibody can also lead to an allosteric effect, modulating the kinetics of binding to target antigen. In the present work, we study the association of a polyhistidine tagged enzyme (phosphoglycerate kinase, PGK) to surface-immobilized anti-His antibodies, finding a significant Charge-Reorganization Allostery (CRA) effect. We further observe that PGK’s negatively charged nucleotide substrates modulate CRA substantially, even though they bind far away from the His-tag–antibody interaction interface. In particular, binding of ATP reduces CRA by more than 50%. The results indicate that CRA is affected by the binding of charged molecules to a protein and provide further insight into the significant role that charge redistribution can play in protein function.
Original languageEnglish
Pages (from-to)2805-2808
Number of pages4
JournalJournal of Physical Chemistry Letters
Issue number11
Early online date12 Mar 2021
StatePublished - 25 Mar 2021


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