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pubmed-article:12618486pubmed:abstractTextWe have addressed the question of whether antigen binding induces a conformational change in the heavy chain constant (C(H)) domain of antibodies using staphylococcal protein A or streptococcal protein G as probes, since these proteins are known to bind to IgG domains such as C(H)1 and C(H)2-C(H)3 domains. Biosensor assays on interactions between these proteins and mouse IgG specific to (4-hydroxy-3-nitrophenyl)acetyl (NP) or their enzymatic fragments conducted in the presence or absence of the hapten, NP-epsilon-aminocaproic acid (NP-Cap), showed that the binding of IgG to these proteins was inhibited by the binding of NP-Cap. The results of isothermal titration calorimetry also revealed that the association constant for the interaction of protein A with IgG2b decreased by the addition of NP-Cap. These results suggested that antigen binding induced conformational changes in binding sites for protein G or protein A located at C(H)1 and C(H)2-C(H)3 domains, respectively.lld:pubmed
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pubmed-article:12618486pubmed:authorpubmed-author:MoriiHisayuki...lld:pubmed
pubmed-article:12618486pubmed:authorpubmed-author:OdaMasayukiMlld:pubmed
pubmed-article:12618486pubmed:authorpubmed-author:AzumaTakachik...lld:pubmed
pubmed-article:12618486pubmed:authorpubmed-author:KozonoHaruoHlld:pubmed
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pubmed-article:12618486pubmed:pagination417-26lld:pubmed
pubmed-article:12618486pubmed:dateRevised2011-11-17lld:pubmed
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pubmed-article:12618486pubmed:year2003lld:pubmed
pubmed-article:12618486pubmed:articleTitleEvidence of allosteric conformational changes in the antibody constant region upon antigen binding.lld:pubmed
pubmed-article:12618486pubmed:affiliationResearch Institute for Biological Sciences, Tokyo University of Science, 2669 Noda, Chiba 278-0022, Japan.lld:pubmed
pubmed-article:12618486pubmed:publicationTypeJournal Articlelld:pubmed
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