抗体-肽复合物的x射线晶体学研究

Stanfield Robyn L., Wilson Ian A.
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引用次数: 24

摘要

用x射线晶体学测定了6种fab -肽复合物的三维结构。肽抗原的大小范围从8到19个残基,包括一个环肽与不寻常的氨基酸侧链。这些结构都是通过分子替代技术确定的,使用已知的Fab结构作为模型,并已改进到中等或高分辨率。这些结构不仅提高了我们对抗体-抗原识别的一般理解,而且有助于确定肽表位的序列和结构特征。肽结构提供了一个框架,以帮助设计肽疫苗或小肽样药物来抑制病毒的功能。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
X-Ray Crystallographic Studies of Antibody–Peptide Complexes

The three-dimensional structures of six Fab-peptide complexes have been determined by X-ray crystallography. The peptide antigens range in size from 8 to 19 residues and include a cyclic peptide with unusual amino acid side chains. The structures were all determined by molecular replacement techniques using known Fab structures as models and have been refined to medium or high resolution. These structures not only have improved our general understanding of antibody-antigen recognition but have aided in the determination of the sequence and structural characteristics of peptide epitopes. The peptide structures provide a framework to aid in the design of peptide vaccines or small peptide-like drugs to inhibit viral function.

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