tert-butyl (2-(4-((6-(2-chloropyridin-3-yl)pyrimidin-4-yl)amino)phenoxy)ethyl)carbamate | 1258507-28-6

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二嗪类
• 英文名称: tert-butyl (2-(4-((6-(2-chloropyridin-3-yl)pyrimidin-4-yl)amino)phenoxy)ethyl)carbamate
• CAS: 1258507-28-6
• 化学式: C₂₂H₂₄ClN₅O₃
• 分子量: 441.917
• InChiKey: MTBSZQGKJJJVIO-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.84
• 重原子数：
  31.0
• 可旋转键数：
  7.0
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.27
• 拓扑面积：
  98.26
• 氢给体数：
  2.0
• 氢受体数：
  7.0

反应信息

• 作为反应物：
  描述：

  tert-butyl (2-(4-((6-(2-chloropyridin-3-yl)pyrimidin-4-yl)amino)phenoxy)ethyl)carbamate 在 1-羟基苯并三唑 、 盐酸-N-乙基-Nˊ-(3-二甲氨基丙基)碳二亚胺 、 三乙胺 、 N,N-二异丙基乙胺 、 三氟乙酸 作用下， 以 二氯甲烷 、 二甲基亚砜 为溶剂， 生成
  参考文献：
  名称：

  Affinity Reagents that Target a Specific Inactive Form of Protein Kinases

  摘要：

  A number of small-molecule inhibitors have been developed that target the catalytic domains of protein kinases that are not in an active conformation. An inactive form that has been observed in several kinases is the DFG-out conformation. This conformation is characterized by an almost 180 degrees rotation of the conserved Asp-Phe-Gly (DFG) motif in the ATP-binding cleft relative to the active form. However, the sequence and structural determinants that allow a kinase to stably adopt the DFG-out conformation are not known. Here, we characterize a series of inhibitors based on a general pharmacophore for this inactive form. We demonstrate that modified versions of these inhibitors can be used to study the thermodynamics and kinetics of ligand binding to DFG-out-adopting kinases and for enriching these kinases from complex protein mixtures.

  DOI：

  10.1016/j.chembiol.2010.01.008
• 作为产物：
  描述：

  2-(4-氨基苯氧基)乙基氨基甲酸叔丁酯 、 4-chloro-6-(2-chloropyridin-3-yl)pyrimidine 以 乙醇 为溶剂， 生成 tert-butyl (2-(4-((6-(2-chloropyridin-3-yl)pyrimidin-4-yl)amino)phenoxy)ethyl)carbamate
  参考文献：
  名称：

  Affinity Reagents that Target a Specific Inactive Form of Protein Kinases

  摘要：

  A number of small-molecule inhibitors have been developed that target the catalytic domains of protein kinases that are not in an active conformation. An inactive form that has been observed in several kinases is the DFG-out conformation. This conformation is characterized by an almost 180 degrees rotation of the conserved Asp-Phe-Gly (DFG) motif in the ATP-binding cleft relative to the active form. However, the sequence and structural determinants that allow a kinase to stably adopt the DFG-out conformation are not known. Here, we characterize a series of inhibitors based on a general pharmacophore for this inactive form. We demonstrate that modified versions of these inhibitors can be used to study the thermodynamics and kinetics of ligand binding to DFG-out-adopting kinases and for enriching these kinases from complex protein mixtures.

  DOI：

  10.1016/j.chembiol.2010.01.008