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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structural insight into nucleotide recognition by human death-associated protein kinase.
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Structural insight into nucleotide recognition by human death-associated protein kinase.

机译：结构洞察核苷酸识别人类的死亡率蛋白激酶。

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摘要

Death-associated protein kinase (DAPK) is a member of the Ca(2+)/calmodulin-regulated family of serine/threonine protein kinases. The role of the kinase activity of DAPK in eukaryotic cell apoptosis and the ability of bioavailable DAPK inhibitors to rescue neuronal death after brain injury have made it a drug-discovery target for neurodegenerative disorders. In order to understand the recognition of nucleotides by DAPK and to gain insight into DAPK catalysis, the crystal structure of human DAPK was solved in complex with ADP and Mg(2+) at 1.85 A resolution. ADP is a product of the kinase reaction and product release is considered to be the rate-limiting step of protein kinase catalytic cycles. The structure of DAPK-ADP-Mg(2+) was compared with a newly determined DAPK-AMP-PNP-Mg(2+) structure and the previously determined apo DAPK structure (PDB code 1jks). The comparison shows that nucleotide-induced changes are localized to the glycine-rich loop region of DAPK.
机译：死亡率蛋白激酶(DAPK)是一个成员Ca (2 +) / calmodulin-regulated家族的丝氨酸/苏氨酸蛋白激酶。激酶活性DAPK的真核细胞细胞凋亡和可利用DAPK的能力抑制剂来拯救大脑神经元死亡后伤害了它的药物目标神经退行性疾病。DAPK理解核苷酸的识别和洞察DAPK催化,晶体结构的人类DAPK解决了复杂的ADP和1.85毫克(2 +)决议。ADP是激酶反应的产物产品版本被认为是病原蛋白激酶催化的一步周期。相比之下,一个新决定DAPK-AMP-PNP-Mg(2 +)结构和之前确定apo DAPK结构(PDB代码1 jks)。比较表明,nucleotide-induced变化是局部的glycine-rich循环DAPK区域。

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