Getzoff E D, Geysen H M, Rodda S J, Alexander H, Tainer J A, Lerner R A
Science. 1987 Mar 6;235(4793):1191-6. doi: 10.1126/science.3823879.
The mechanisms of antibody binding to a protein were studied by an analysis of specific amino acid residues critical to nine antigenic sites on myohemerythrin. Rabbit antisera to the whole protein were assayed for binding to more than 1500 distinct peptide analogs differing from the protein sequence by single amino acid replacements. The results, combined with information from the three-dimensional crystallographic structure, were used to evaluate probable mechanisms of antibody binding at individual sites. The data from all sites examined indicate that initial binding to solvent-exposed amino acid residues may promote local side-chain displacements and thereby allow the participation of other, previously buried, residues.
通过分析对肌红蛋白九个抗原位点至关重要的特定氨基酸残基,研究了抗体与蛋白质结合的机制。检测了针对全蛋白的兔抗血清与1500多种与蛋白质序列有单个氨基酸替换差异的不同肽类似物的结合情况。将这些结果与三维晶体结构信息相结合,用于评估各个位点抗体结合的可能机制。所有检测位点的数据表明,与溶剂暴露的氨基酸残基的初始结合可能促进局部侧链位移,从而使其他先前埋藏的残基得以参与。