Structure-based functional site recognition for p21-activated kinase 4.
Structure-based functional site recognition for p21-activated kinase 4.
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p21 激活激酶 4 基于结构的功能位点识别。
DOI：
10.1007/s12272-013-0165-8
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发表时间：
2013
影响因子：
6.7
通讯作者：
Cheng Mao-Sheng
中科院分区：
文献类型：
--
作者：
Wang Jian;Wang Gang;Sha Yu;Zhao Dong-Mei;Li Feng;Cheng Mao-Sheng
摘要最近，人们正在开发许多分子建模方法，以更好地理解蛋白质折叠的原理。在本研究中，完全灵活的二核苷酸 d(pApA)、d(pApC)、d(pApG)、d(pApT)、d(pCpA)、d(pCpC)、d(pCpG)、d(pCpT)、d(pGpA)、d(pGpC)、d(pGpG)、 d(pGpT)、d(pTpA)、d(pTpC)、d(pTpG) 和 d(pTpT) 对接至 p21 激活激酶 4 (PAK4) 激酶结构域的表面。结果表明，自动对接是识别PAK4功能位点的有用工具，并且可以为先前实验获得的相互作用数据提供理论基础。因此，基于结构的对接与完全灵活的二核苷酸探针可能是预测和注释酶功能位点的好工具。图形摘要
AbstractRecently, many molecular modeling methods are being developed to better understand the principles underlying protein folding. In the present study, fully flexible dinucleotides d(pApA), d(pApC), d(pApG), d(pApT), d(pCpA), d(pCpC), d(pCpG), d(pCpT), d(pGpA), d(pGpC), d(pGpG), d(pGpT), d(pTpA), d(pTpC), d(pTpG) and d(pTpT) were docked onto the surface of p21-activated kinase 4 (PAK4) kinase domain. The results showed that automated docking was a useful tool to identify the functional sites of PAK4 and it may provide a theoretical basis for the interaction data obtained from previous experiments. Therefore, structure-based docking with fully flexible dinucleotide probes might be a good tool to predict and annotate the functional sites of enzymes.Graphical Abstract