ENERGY-TRANSFER BETWEEN 2 PEPTIDES BOUND TO ONE MHC CLASS-II MOLECULE

被引：40

作者：

TAMPE, R ^{[1
]}

CLARK, BR ^{[1
]}

MCCONNELL, HM ^{[1
]}

机构：

[1] ANERGEN INC,REDWOOD CITY,CA 94063

来源：

SCIENCE | 1991年 / 254卷 / 5028期

关键词：

D O I：

10.1126/science.1656526

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 17-amino acid peptide from chicken ovalbumin, Ova(323-339), was labeled at the amino terminus with fluorescein [FOva(323-339)] and near the carboxyl terminus with Texas Red [AcOva(323-338)KTR]. Fluorescence spectroscopy was carried out on resolved electrophoretic bands on nonreducing polyacrylamide gels derived from incubation mixtures containing major histocompatibility complex (MHC) class II molecules IA(d) and the FOva(323-339)- and AcOva(323-338)KTR-labeled peptides. Energy transfer between fluorescein and Texas Red was observed in the "floppy" alpha-beta heterodimer band, but not in the "compact" alpha-beta heterodimer band. Energy transfer was detected between the truncated peptides FOva(323-328)CONH2 and AcOva(331-338)KTR in both the compact alpha-beta and floppy alpha-beta gel bands. The energy-transfer data suggest that the two binding sites of floppy alpha-beta arise from splitting apart a putative large, single binding site region in compact alpha-beta.

引用

页码：87 / 89

页数：3

共 17 条

[1] ANALYSIS OF PEPTIDE BINDING PATTERNS IN DIFFERENT MAJOR HISTOCOMPATIBILITY COMPLEX T-CELL RECEPTOR COMPLEXES USING PIGEON CYTOCHROME C-SPECIFIC T-CELL HYBRIDOMAS - EVIDENCE THAT A SINGLE PEPTIDE BINDS MAJOR HISTOCOMPATIBILITY COMPLEX IN DIFFERENT CONFORMATIONS [J].