Identification of a key element for hydrogen-bonding patterns between protein kinases and their inhibitors
Identification of a key element for hydrogen-bonding patterns between protein kinases and their inhibitors
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DOI：
10.1002/prot.22207
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发表时间：
2008-12-01
影响因子：
2.9
通讯作者：
Niimi, Tatsuya
中科院分区：
文献类型：
--
作者：
Katayama, Naoko;Orita, Masaya;Niimi, Tatsuya
在这篇文章中，我们报告的晶体结构的抑制剂激酶复合物中，具有不同的结合方向和氢键模式与细胞外信号调节激酶2和胰岛素受体酪氨酸激酶。我们的晶体学研究，以及蛋白质数据库中532个激酶坐标的序列和结构分析表明，这里描述的“特异性接头”的长度是蛋白质激酶及其抑制剂之间氢键模式的关键结构元素。
In this article, we report crystal structures for inhibitor-kinase complexes in which the inhibitor has different binding orientations and hydrogen-bonding patterns with extracellular-signal regulated kinase 2 and insulin receptor tyrosine kinase. Our crystallographic studies, and sequence and structural analyses of 532 coordinates of kinases held in the Protein Data Bank, suggest that the length of the "specificity linker" described here is a key structural element of the hydrogen-bonding patterns between protein kinases and their inhibitors.