Antigen recognition by conformational selection

被引:104
作者
Berger, C [1 ]
Weber-Bornhauser, S [1 ]
Eggenberger, J [1 ]
Hanes, J [1 ]
Plückthun, A [1 ]
Bosshard, HR [1 ]
机构
[1] Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland
关键词
antigen-antibody recognition; antibody specificity; conformational selection; induced fit; binding kinetic; transcription factor GCN4;
D O I
10.1016/S0014-5793(99)00458-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Conformational adaptation between antigen and antibody can modulate the antibody specificity. The phenomenon has often been proposed to result from an 'induced fit', which implies that the binding reaction induces a conformational change in the antigen and the antibody. Thus, an 'induced fit' requires initial complex formation followed by a conformational change in the complex. However, an antibody may select those antigen molecules that happen to be in a fitting conformational state. This leads to the same end result as an induced fit. Here, we demonstrate conformational selection by a single chain antibody fragment, raised against a random coil variant of the leucine zipper domain of transcription factor GCN4, when it cross-reacts with the wild-type dimeric leucine zipper. Kinetic and equilibrium data show that the single chain antibody fragment fragment selects monomeric peptides from the population in equilibrium with the leucine zipper dimer, (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:149 / 153
页数:5
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