Höhne W E, Küttner G, Kiessig S, Hausdorf G, Grunow R, Winkler K, Wessner H, Giessmann E, Stigler R, Schneider-Mergener J
Institut für Biochemie, Medizinische Fakultät (Charité), Humboldt-Universität, Berlin, Germany.
Mol Immunol. 1993 Sep;30(13):1213-21. doi: 10.1016/0161-5890(93)90140-7.
The interaction of a murine monoclonal antibody (CB 4-1) against the core protein p24 of HIV-1 with its peptide antigen was studied in detail. The amino acid sequence of the variable regions of the heavy and light chain as derived from DNA sequencing was used to model the structure of the antigen binding region on the basis of reported Fab structures from the Brookhaven Protein Data Base. A linear peptide epitope responsible for the p24 binding to the antibody was determined by peptide scan. Subsequent N- and C-terminal truncation of the corresponding sequence region as well as amino acid substitutions were performed to recognize the epitope and the amino acid residues critical for antibody binding. These data were used to derive a structural model of the peptide-antibody interaction.
详细研究了一种针对HIV-1核心蛋白p24的鼠单克隆抗体（CB 4-1）与其肽抗原的相互作用。通过DNA测序获得的重链和轻链可变区的氨基酸序列，基于布鲁克海文蛋白质数据库中报道的Fab结构，用于模拟抗原结合区的结构。通过肽扫描确定了负责p24与抗体结合的线性肽表位。随后对相应序列区域进行N端和C端截短以及氨基酸替换，以识别表位和对抗体结合至关重要的氨基酸残基。这些数据被用于推导肽-抗体相互作用的结构模型。
