Burmeister W P, Gastinel L N, Simister N E, Blum M L, Bjorkman P J
Division of Biology 156-29, California Institute of Technology, Pasadena 91125.
Nature. 1994 Nov 24;372(6504):336-43. doi: 10.1038/372336a0.
The three-dimensional structure of the rat neonatal Fc receptor (FcRn) is similar to the structure of molecules of the major histocompatibility complex (MHC). The counterpart of the MHC peptide-binding site is closed in FcRn, making the FcRn groove incapable of binding peptides. A dimer of FcRn heterodimers seen in the crystals may represent a receptor dimer that forms when the Fc portion of a single immunoglobulin binds. An alternative use of the MHC fold for immune recognition is indicated by the FcRn and FcRn/Fc co-crystal structures.
大鼠新生Fc受体(FcRn)的三维结构与主要组织相容性复合体(MHC)分子的结构相似。FcRn中MHC肽结合位点的对应部分是封闭的,使得FcRn凹槽无法结合肽。晶体中所见的FcRn异二聚体二聚体可能代表当单个免疫球蛋白的Fc部分结合时形成的受体二聚体。FcRn和FcRn/Fc共晶体结构表明了MHC折叠在免疫识别中的另一种用途。