Valdez B C, Busch R K, Larson R G, Busch H
Department of Pharmacology, Baylor College of Medicine, Houston, Texas 77030.
Cancer Res. 1990 May 1;50(9):2704-7.
An epitope region, located at amino acid residues 173-180 (EAAA-GIQW), of a human cell proliferation-associated nucleolar antigen, P120, has been defined by mutational analysis and competition assays. A synthetic peptide corresponding to this epitope region completely blocks the binding of the anti-P120 antibody to Escherichia coli-expressed P120 and the HeLa nucleolar P120 protein. Adjacent peptides lack inhibitory effects. The antigenic site includes a hydrophilic residue and a hydrophobic stretch. The glutamyl and tryptophanyl residues in this region make major contributions to the binding of P120 to its antibody, since peptides lacking either the glutamyl or the tryptophanyl residue do not block the antibody binding to the P120 antigen. This study provides a basis for drug design for specific binding to the epitope region of the P120 protein.
通过突变分析和竞争试验，已确定人细胞增殖相关核仁抗原P120位于氨基酸残基173 - 180（EAAA - GIQW）的一个表位区域。对应于该表位区域的合成肽完全阻断抗P120抗体与大肠杆菌表达的P120以及HeLa细胞核仁P120蛋白的结合。相邻肽段无抑制作用。该抗原位点包括一个亲水性残基和一个疏水区段。该区域中的谷氨酰基和色氨酰基残基对P120与其抗体的结合起主要作用，因为缺少谷氨酰基或色氨酰基残基的肽段不能阻断抗体与P120抗原的结合。本研究为设计与P120蛋白表位区域特异性结合的药物提供了依据。
