MOST RESIDUES ON THE FLOOR OF THE ANTIGEN-BINDING SITE OF THE CLASS-I MHC MOLECULE H-2KD INFLUENCE PEPTIDE PRESENTATION

被引：14

作者：

JAULIN, C

ROMERO, P

LUESCHER, IF

CASANOVA, JL

PROCHNICKACHALUFOUR, A

LANGLADEDEMOYEN, P

MARYANSKI, JL

KOURILSKY, P

机构：

[1] LUDWIG INST CANC RES,CH-1066 EPALINGES,SWITZERLAND

[2] INST PASTEUR,UNITE BIOL MOLEC GENE,F-75724 PARIS 15,FRANCE

[3] INST PASTEUR,UNITE INFORMAT SCI,F-75724 PARIS 15,FRANCE

来源：

INTERNATIONAL IMMUNOLOGY | 1992年 / 4卷 / 08期

关键词：

HISTOCOMPATIBILITY ANTIGENS; PEPTIDE BINDING; PHOTOAFFINITY LABELING; SITE-DIRECTED MUTAGENESIS; SURFACE EXPRESSION; T-CELL RECOGNITION;

D O I：

10.1093/intimm/4.8.945

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

A panel of 15 single alanine substitutions on the floor of the peptide binding groove of the murine class I histocompatibility molecule H-2K(d) has been analyzed. All but two mutant molecules were expressed on the cell surface, and were tested for peptide binding and presentation to specific cytotoxic T lymphocytes. Eleven out of 13 mutant molecules appeared to be functionally altered. Five of the substituted residues were involved in the presentation of all peptides tested. Three participated in the presentation of certain peptides but not others. Three other residues participated in epitope formation through indirect interactions. Only two mutations had no detectable effect.

引用

收藏

页码：945 / 953

页数：9

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