THE BINDING-AFFINITY AND DISSOCIATION RATES OF PEPTIDES FOR CLASS-I MAJOR HISTOCOMPATIBILITY COMPLEX-MOLECULES

被引：195

作者：

CERUNDOLO, V ^{[1
]}

ELLIOTT, T ^{[1
]}

ELVIN, J ^{[1
]}

BASTIN, J ^{[1
]}

RAMMENSEE, HG ^{[1
]}

TOWNSEND, A ^{[1
]}

机构：

[1] MAX PLANCK INST BIOL, IMMUNGENET ABT, W-7400 TUBINGEN, GERMANY

来源：

EUROPEAN JOURNAL OF IMMUNOLOGY | 1991年 / 21卷 / 09期

关键词：

D O I：

10.1002/eji.1830210915

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Peptides of various lengths derived from the influenza nucleoprotein (NP) bind to H-2D(b) class I molecules with affinities at 4-degrees-C between approximately 3 x 10(5) - approximately 3 x 10(7) M-1. The peptide with the highest affinity corresponds to the sequence of nine amino acids (NP366-374) recently isolated from cells infected with influenza. This peptide forms stable complexes with half-lives > 110 h at 4-degrees-C, 39 h at 22-degrees-C and 3 h at 37-degrees-C. Small increases in length of the peptide greatly reduce the stability of the complex (t1/2 approximately 1-10 h at 4-degrees-C). These results may explain the homogeneous length of peptides isolated from class I molecules formed in vivo, and suggest that class I and II may differ in their dependence on the length of peptides for the formation of stable complexes.

引用

页码：2069 / 2075

页数：7

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