CRYSTAL-STRUCTURE AT 2.2-ANGSTROM RESOLUTION OF THE MHC-RELATED NEONATAL FC RECEPTOR

被引：267

作者：

BURMEISTER, WP

GASTINEL, LN

SIMISTER, NE

BLUM, ML

BJORKMAN, PJ

机构：

[1] CALTECH,DEPT BIOL,PASADENA,CA 91125

[2] CALTECH,HOWARD HUGHES MED INST,PASADENA,CA 91125

[3] BRANDEIS UNIV,DEPT BIOL,WALTHAM,MA 02254

[4] BRANDEIS UNIV,ROSENSTIEL BASIC MED SCI RES CTR,WALTHAM,MA 02254

来源：

NATURE | 1994年 / 372卷 / 6504期

关键词：

D O I：

10.1038/372336a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The three-dimensional structure of the rat neonatal Fe 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.

引用

页码：336 / 343

页数：8

共 50 条

[1]

AHOUSE JJ, 1993, J IMMUNOL, V151, P6076

[2] STRUCTURAL BASIS OF THE IGE-FCERI INTERACTION [J].