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CD2 is a T cell surface molecule that enhances T and natural killer cell function by binding its ligands CD58 (humans) and CD48 (rodents) on antigen-presenting or target cells. Here we show that the CD2/CD58 interaction is enthalpically driven and accompanied by unfavorable entropic changes. Taken together with structural studies, this indicates that binding is accompanied by energetically significant conformational adjustments. Despite having a highly charged binding interface, neither the affinity nor the rate constants of the CD2/CD58 interaction were affected by changes in ionic strength, indicating that long-range electrostatic forces make no net contribution to binding.

Original publication




Journal article


J Biol Chem

Publication Date





13160 - 13166


Animals, Antigens, CD, CD2 Antigens, CD48 Antigen, CD58 Antigens, Humans, Killer Cells, Natural, Osmolar Concentration, Protein Binding, Protein Structure, Quaternary, Rodentia, Static Electricity, Surface Plasmon Resonance, T-Lymphocytes