Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor.
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.
Division of Biology 156-29, California Institute of Technology, Pasadena 91125.
W P
WP
Burmeister
L N
LN
Gastinel
N E
NE
Simister
M L
ML
Blum
P J
PJ
Bjorkman
D000818:Animals; D000831:Animals, Newborn / Q000276:immunology*; D005075:Biological Evolution; D003196:Computer Graphics; D018360:Crystallography, X-Ray; D015395:Histocompatibility Antigens Class I / Q000737:chemistry*; D007141:Immunoglobulin Fc Fragments / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D051381:Rats; D011961:Receptors, Fc / Q000737:chemistry* / Q000378:metabolism
D015395:Histocompatibility Antigens Class I; D007141:Immunoglobulin Fc Fragments; D011961:Receptors, Fc