Please use this identifier to cite or link to this item: https://ahro.austin.org.au/austinjspui/handle/1/13640
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dc.contributor.authorHulett, M Den
dc.contributor.authorHogarth, P Marken
dc.date.accessioned2015-05-16T03:31:19Z
dc.date.available2015-05-16T03:31:19Z
dc.date.issued1998-10-01en
dc.identifier.citationMolecular Immunology; 35(14-15): 989-96en
dc.identifier.govdoc9881694en
dc.identifier.otherPUBMEDen
dc.identifier.urihttp://ahro.austin.org.au/austinjspui/handle/1/13640en
dc.description.abstractFcgammaRI (CD64) is functionally unique as it is the only FcgammaR able to bind monomeric IgG with high affinity. FcgammaRI is also structurally distinct, containing an extracellular Ig-interactive region of three Ig-like domains in contrast to the two domains of the low affinity receptors FcgammaRII and FcgammaRIII. Previous studies have demonstrated that the third domain of FcgammaRI plays a crucial role in high affinity IgG binding of the receptor, with the first and second domains together forming a low affinity IgG binding motif. In this study the individual functional contributions of the first and second domains of FcgammaRI to IgG binding have been investigated. Chimeric FcgammaR were generated by exchanging extracellular domains between mouse FcgammaRI and the structurally related yet distinct low affinity receptor for IgG, mouse FcgammaRII. The replacement of both domains 1 and 2 of FcgammaRI with domains 1 and 2 of FcgammaRII results in a dramatic change in IgG binding characteristics, as this receptor loses the capacity to bind monomeric IgG with high affinity and also demonstrates a broader specificity (binding not only IgG2a but also IgG1 and 2b. IgG3 was not tested). However, the substitution of FcgammaRII domain 2 of this chimeric receptor with domain 2 of FcgammaRI (generating a chimeric receptor with domain 1 of FcgammaRII linked to domains 2 and 3 of FcgammaRI) was found to reconstitute the specific high affinity monomeric IgG2a binding of wild-type FcgammaRI, albeit with a slightly reduced affinity (1.8-fold lower than wild-type FcgammaRI). These findings suggest that it is the specific interaction between domains 2 and 3 of FcgammaRI, with domain 1 playing a supporting role in maintaining the conformational stability of the receptor, that is the major structural requirement to confer the unique Ig binding characteristics of FcgammaRI.en
dc.language.isoenen
dc.subject.otherAnimalsen
dc.subject.otherAntibody Affinity.physiologyen
dc.subject.otherAntibody Specificityen
dc.subject.otherCOS Cells.cytologyen
dc.subject.otherImmunoglobulin G.immunologyen
dc.subject.otherMembrane Proteins.immunologyen
dc.subject.otherMiceen
dc.subject.otherProtein Structure, Tertiaryen
dc.subject.otherReceptors, IgG.biosynthesis.chemistry.immunologyen
dc.subject.otherRecombinant Fusion Proteins.biosynthesis.immunologyen
dc.titleThe second and third extracellular domains of FcgammaRI (CD64) confer the unique high affinity binding of IgG2a.en
dc.typeJournal Articleen
dc.identifier.journaltitleMolecular immunologyen
dc.identifier.affiliationThe Austin Research Institute, Austin Hospital, Heidelberg, Victoria, Australiaen
dc.description.pages989-96en
dc.relation.urlhttps://pubmed.ncbi.nlm.nih.gov/9881694en
dc.type.austinJournal Articleen
item.openairetypeJournal Article-
item.fulltextNo Fulltext-
item.languageiso639-1en-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
item.cerifentitytypePublications-
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