3-(naphthalen-2-ylmethylthio)thiophene-2-carboxylic acid | 1336982-43-4

• 分子结构分类: 有机化合物 - 苯类化合物 - 萘
• 英文名称: 3-(naphthalen-2-ylmethylthio)thiophene-2-carboxylic acid
• 英文别名: 3-(Naphthalen-2-ylmethylsulfanyl)thiophene-2-carboxylic acid
• CAS: 1336982-43-4
• 化学式: C₁₆H₁₂O₂S₂
• 分子量: 300.402
• InChiKey: KGAVOXKNHSTTFM-UHFFFAOYSA-N

计算性质

• 辛醇/水分配系数(LogP)：
  4.7
• 重原子数：
  20
• 可旋转键数：
  4
• 环数：
  3.0
• sp3杂化的碳原子比例：
  0.06
• 拓扑面积：
  90.8
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  3-ethoxythiocarbonylsulfanylthiophene-2-carboxylic acid methyl ester 在 sodium methylate 、 sodium hydroxide 作用下， 以 甲醇 、 乙醇 、 二甲基亚砜 为溶剂， 反应 5.0h， 生成 3-(naphthalen-2-ylmethylthio)thiophene-2-carboxylic acid
  参考文献：
  名称：

  Small Molecule Receptor Protein Tyrosine Phosphatase γ (RPTPγ) Ligands That Inhibit Phosphatase Activity via Perturbation of the Tryptophan–Proline–Aspartate (WPD) Loop

  摘要：

  Protein tyrosine phosphatases (PTPs) catalyze the dephosphorylation of tyrosine residues, a process that involves a conserved tryptophan-proline-aspartate (WPD) loop in catalysis. In previously determined structures of PTPs, the WPD-loop has been observed in either an "open" conformation or a "closed" conformation. In the current work, X-ray structures of the catalytic domain of receptor-like protein tyrosine phosphatase gamma (RPTP gamma) revealed a ligand-induced "superopen" conformation not previously reported for PTPs. In the superopen conformation, the ligand acts as an apparent competitive inhibitor and binds in a small hydrophobic pocket adjacent to, but distinct from, the active site. In the open and closed WPD-loop conformations of RPTP gamma, the side chain of Trp1026 partially occupies this pocket. In the superopen conformation, Trp1026 is displaced allowing a 3,4-dichlorobenzyl substituent to occupy this site. The bound ligand prevents closure of the WPD-loop over the active site and disrupts the catalytic cycle of the enzyme.

  DOI：

  10.1021/jm2003766