Identification of critical IgG binding epitopes on the neonatal Fc receptor.
Identification of critical IgG binding epitopes on the neonatal Fc receptor.
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新生儿 Fc 受体上关键 IgG 结合表位的鉴定。
DOI：
10.1006/jmbi.1997.1388
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Bjorkman,PJ
中科院分区：
文献类型：
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作者：
Vaughn,DE;Milburn,CM;Penny,DM;Martin,WL;Johnson,JL;Bjorkman,PJ
新生儿Fc受体（FcRn）在胎儿或新生儿获得被动免疫期间与母体免疫球蛋白G（IgG）结合。FcRn还结合IgG并使其返回血流，从而保护IgG免受默认降解途径的影响。生物传感器测定已用于表征可溶形式的大鼠FcRn与IgG的相互作用，并证明FcRn二聚化和固定化对于再现体内结合特征是必要的。在这里，我们报告了几个FcRn氨基酸取代，破坏其对IgG的亲和力，并检查在FcRn二聚体界面的残基的改变的影响。这些氨基酸的作用进行了讨论的背景下，先前报道的大鼠FcRn和FcRn与IgG的Fc部分的复合物的结构。
The neonatal Fc receptor (FcRn) binds maternal immunoglobulin G (IgG) during the acquisition of passive immunity by the fetus or newborn. FcRn also binds IgG and returns it to the bloodstream, thus protecting IgG from a default degradative pathway. Biosensor assays have been used to characterize the interaction of a soluble form of rat FcRn with IgG, and demonstrate that FcRn dimerization and immobilization are necessary to reproduce in vivo binding characteristics. Here, we report the identification of several FcRn amino acid substitutions that disrupt its affinity for IgG and examine the effect of alteration of residues at the FcRn dimer interface. The role of these amino acids is discussed in the context of the previously reported structures of rat FcRn and a complex of FcRn with the Fc portion of IgG.