The contribution of conformational adjustments and long-range electrostatic forces to the CD2/CD58 interaction.

Journal article

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.

Authors: Kearney, A; Avramovic, A; Castro, M; Carmo, A; Davis, S

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 282
• Issue: 18
• Pages: 13160-13166
• Publication date: 2007-05-01
• DOI: 10.1074/jbc.m700829200
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Protein Structure, Quaternary; Killer Cells, Natural; T-Lymphocytes; Antigens, CD2; Protein Binding; Osmolar Concentration; Animals; Surface Plasmon Resonance; Antigens, CD58; Rodentia; Humans; Static Electricity; Antigens, CD