R^(49)A^(50)RGDN^(54)P^(55)突变成I^(49)P^(50)RGDM^(54)P^(55)对华丽蛇毒素活性的影响(英文)

Effect of Elegantin Mutagenesis (R^(49)A^(50)RGDN^(54)P^(55) to I^(49)P^(50)RGDM^(54)P^(55)) on its Activity

用基因点突变技术将已知具有强抑制血小板凝集作用的去整合蛋白———kistrin的RGD袢区IPRGDMP替换抑制血小板凝集作用较弱的elegantinRGD袢相应部位的RARGDNP,重构一个新的杂合的去整合蛋白,然后,分析该杂合蛋白对血小板凝集的抑制作用。结果表明,重组的杂合去整合蛋白比野生型elegantin具有更强的抑制血小板凝集活性。推测RGD顺序两翼的氨基酸残基在保持去整合蛋白的结构和功能中起重要作用。

To study further the action of the amino acid residues flanking the RGD sequence of disintegrins, the sequence within elegantin RARGDNP was changed by mutagenesis to IPRGDMP, thereby resembling the corresponding IPRGDMP sequence in kistrin. The results showed that this change RARGDNP→IPRGDMP clearly increased the activity of elegantin as an inhibitor of platelet aggregation. These data further suggested the importance of the amino acid residues flanking RGD sequence on the structure and function of disintegrins.