机构:Dept of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston
DENAGEL, DC
PIERCE, SK
论文数: 0引用数: 0
h-index: 0
机构:Dept of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston
PIERCE, SK
机构:
[1] Dept of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston
来源:
IMMUNOLOGY TODAY
|
1992年
/
13卷
/
03期
关键词:
D O I:
10.1016/0167-5699(92)90147-Y
中图分类号:
R392 [医学免疫学];
Q939.91 [免疫学];
学科分类号:
100102 ;
摘要:
The assembly of peptide-MHC-class-II molecule complexes by antigen-presenting cells is far more efficient than would be predicted from studies of peptide binding to purified MHC class II molecules in vitro. One possible explanation for this discrepancy is that proteins in the antigen-presenting cell facilitate the assembly process. Here, Diane DeNagel and Susan Pierce present the case for involvement of members of the chaperone/heat shock protein 70 family in the intracellular assembly of processed-antigen-MHC-class-II-molecule complexes.