Antigen recognition by conformational selection

FEBS Letters

Weber-Bornhauser, Susanne¹  Eggenberger, Jolanda¹  Hanes, Jozef¹  Berger, Christine¹  Bosshard, Hans Rudolf¹  Plückthun, Andreas¹ 

[1] Biochemisches Institut der Universität, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland

关键词: Antigen-antibody recognition;    Antibody specificity;    Conformational selection;    Induced fit;    Binding kinetic;    Transcription factor GCN4;    AP-1;    activation protein 1;    CRE;    cyclic AMP response element ATGACGTCAT;    CD;    circular dichroism;    GCN4;    general control of amino acid synthesis non-derepressible mutant 4;    PBS;    phosphate-buffered saline;    scFv;    single chain antibody fragment;   

DOI  :  10.1016/S0014-5793(99)00458-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown