 |
|
Title
|
|
Crystal structure at 2.2 A resolution of the MHC-related neonatal Fc receptor.
|
|
|
Authors
|
|
W.P.Burmeister,
L.N.Gastinel,
N.E.Simister,
M.L.Blum,
P.J.Bjorkman.
|
|
|
Ref.
|
|
Nature, 1994,
372,
336-343.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
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.
|
|
|
|