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抗体催化剂的结构多样性。

Structural diversity of antibody catalysts.

作者信息

Golinelli-Pimpaneau Béatrice

机构信息

Laboratoire d'Enzymologie et Biochimie Structurales, CNRS Bât. 34, 1 Avenue de la Terrasse, 91198 Gif-sur-Yvette Cedex, France.

出版信息

J Immunol Methods. 2002 Nov 1;269(1-2):157-71. doi: 10.1016/s0022-1759(02)00240-5.

DOI:10.1016/s0022-1759(02)00240-5
PMID:12379360
Abstract

The structural diversity of the immune response may be considerably restricted by the structure of the hapten used to elicit catalytic antibodies. The ligand-binding mode and the shapes of the binding pockets of hydrolytic antibodies induced to different transition-state analogs that contain an unsubstituted arylphosphonate group are very similar. Moreover, antibodies elicited against a single transition state analog evolve from a single germline gene or different precursors, depending on the nature of the hapten. Germline antibodies seem to adopt multiple conformations with antigen binding, together with somatic mutation stabilizing the conformation with optimum complementarity to antigen.

摘要

用于引发催化抗体的半抗原的结构可能会极大地限制免疫反应的结构多样性。诱导产生的针对含有未取代芳基膦酸酯基团的不同过渡态类似物的水解抗体的配体结合模式和结合口袋形状非常相似。此外,针对单一过渡态类似物产生的抗体是从单个种系基因还是不同的前体进化而来,这取决于半抗原的性质。种系抗体似乎在与抗原结合时会采用多种构象,同时体细胞突变会稳定与抗原具有最佳互补性的构象。

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Structural diversity of antibody catalysts.抗体催化剂的结构多样性。
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Structural insights into the evolution of an antibody combining site.抗体结合位点进化的结构洞察
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Analysis of hapten binding and catalytic determinants in a family of catalytic antibodies.催化抗体家族中半抗原结合和催化决定因素的分析。
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