PMID- 11544262 OWN - NLM STAT- MEDLINE DCOM- 20020110 LR - 20210209 IS - 0021-9258 (Print) IS - 0021-9258 (Linking) VI - 276 IP - 48 DP - 2001 Nov 30 TI - The human low affinity Fcgamma receptors IIa, IIb, and III bind IgG with fast kinetics and distinct thermodynamic properties. PG - 44898-904 AB - Fcgamma receptors (FcgammaRs) are expressed on all immunologically active cells. They bind the Fc portion of IgG, thereby triggering a range of immunological functions. We have used surface plasmon resonance to analyze the kinetic and thermodynamic properties of the interactions between the ectodomains of human low affinity FcgammaRs (FcgammaRIIa, FcgammaRIIb, and FcgammaRIIIb-NA2) and IgG1 or the Fc fragment of IgG1. All three receptors bind Fc or IgG with similarly low affinities (K(D) approximately 0.6-2.5 microm) and fast kinetics, suggesting that FcgammaR-mediated recognition of aggregated IgG and IgG-coated particles or cells is mechanistically similar to cell-cell recognition. Interestingly, the Fc receptors exhibit distinct thermodynamic properties. Whereas the binding of the FcgammaRIIa and FcgammaRIIb to Fc is driven by favorable entropic and enthalpic changes, the binding of FcgammaRIII is characterized by highly unfavorable entropic changes. Although the structural bases for these differences remain to be determined, they suggest that the molecular events coupled to the binding differ among the low affinity FcgammaRs. FAU - Maenaka, K AU - Maenaka K AD - Structural Biology Center, National Institute of Genetics, Mishima, Shizuoka 411-8540, Japan. kmaenaka@lab.nig.ac.jp FAU - van der Merwe, P A AU - van der Merwe PA FAU - Stuart, D I AU - Stuart DI FAU - Jones, E Y AU - Jones EY FAU - Sondermann, P AU - Sondermann P LA - eng PT - Journal Article PT - Research Support, Non-U.S. Gov't DEP - 20010905 PL - United States TA - J Biol Chem JT - The Journal of biological chemistry JID - 2985121R RN - 0 (Antigens, CD) RN - 0 (FCGR3B protein, human) RN - 0 (Fc gamma receptor IIA) RN - 0 (Fc gamma receptor IIB) RN - 0 (GPI-Linked Proteins) RN - 0 (Immunoglobulin G) RN - 0 (Receptors, IgG) SB - IM MH - Antigens, CD/chemistry/*metabolism MH - Entropy MH - GPI-Linked Proteins MH - Humans MH - Immunoglobulin G/metabolism MH - Kinetics MH - Models, Molecular MH - Protein Binding MH - Protein Conformation MH - Protein Structure, Tertiary MH - Receptors, IgG/chemistry/*metabolism MH - Surface Plasmon Resonance MH - Temperature MH - Thermodynamics MH - Time Factors EDAT- 2001/09/07 10:00 MHDA- 2002/01/11 10:01 CRDT- 2001/09/07 10:00 PHST- 2001/09/07 10:00 [pubmed] PHST- 2002/01/11 10:01 [medline] PHST- 2001/09/07 10:00 [entrez] AID - S0021-9258(19)82693-5 [pii] AID - 10.1074/jbc.M106819200 [doi] PST - ppublish SO - J Biol Chem. 2001 Nov 30;276(48):44898-904. doi: 10.1074/jbc.M106819200. Epub 2001 Sep 5.