酪氨酸315、319和493磷酸化后ZAP-70激活的结构基础

IF 0.1 Q4 MULTIDISCIPLINARY SCIENCES
V. Urban, V. Veresov
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引用次数: 0

摘要

ZAP-70(Zeta链相关蛋白激酶70)是调节适应性免疫反应的关键激酶。Zap-70的作用是将其SH2结构域与T细胞相关的CD3ζ蛋白结合,从而传递由主要组织相容性复合体与T细胞受体相互作用诱导的T细胞激活信号。已经证实,对于ZAP-70激酶的激活,需要Tyr315、Tyr319和Tyr493的磷酸化,然而其机制尚不清楚。在本研究中,我们使用结构建模的工具来阐明ZAP-70的激活机制。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structural basis of ZAP-70 activation upon phosphorylation of tyrosines 315, 319 and 493
ZAP-70 (Zeta-chain-Associated Protein kinase 70) is a key kinase in the regulation of the adaptive immune response. Zap-70 acts by binding its SH2-domains to the T-cell-associated CD3ζ protein, thus transmitting a T-cell activation signal induced by the interaction of Major Histocompatibility Complex with T-cell Receptor. It has been established that for ZAP-70 kinase activation, the phosphorylation of Tyr315, Tyr319, and Tyr493 is required, however the mechanisms are unclear. In the present study, we use the tools of structural modeling to elucidate the ZAP-70 activation mechanisms.
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来源期刊
DOKLADY NATSIONALNOI AKADEMII NAUK BELARUSI
DOKLADY NATSIONALNOI AKADEMII NAUK BELARUSI MULTIDISCIPLINARY SCIENCES-
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