Effect of single mutagenesis on the binding pocket of canine estrogen receptor alpha: Structure and binding affinity
作者: Waraphan Toniti Aekkapot Chamkasem Panpanga Sangsuriya Pranom Puchadapirom
刊名: Advances in Modern Oncology Research, 2016, Vol.2 (2)
来源数据库: PiscoMed Publishing Pte. Ltd
DOI: 10.18282/amor.v2.i2.79
关键词: estrogen receptor alphacaninemutagenesisbinding affinity
原始语种摘要: Hormone-related mammary gland tumors are among the most commonly diagnosed neoplasms in female dogs. Estrogen enacts its biological roles through specific receptors known as estrogen receptors (ER). In human medicine, anti-estrogen therapy has become the gold standard in ER-positive breast tumors’ therapeutic regimen. The binding pocket of the canine estrogen receptor alpha (cERα) ligand binding domain comprises of three key amino acid residues including E354, G522 and L526, which stabilize the cERα-E2 interaction via hydrogen bonding. The side chain of E354 shares hydrogen bond interaction with the A ring of its natural ligand E2, whereas the main chain of G522 and L526 interact with the E2-D ring. The single mutation of the E354 aberrant, along with the hydrogen bond interaction between...
全文获取路径: PiscoMed Publishing  (合作)

  • interaction 相互酌
  • binding 装订
  • whereas 鉴于
  • chain 
  • estrogen 雌激素
  • might 能力
  • further 进一步
  • female 女性的
  • known 己知
  • stabilize 稳定