Crystal structure and transient dimerization for the FKBP12 protein from the pathogenic fungus Candida auris
作者: Qamar BashirZhong LiHongmin LiDavid M. LeMasterGriselda Hernández
作者单位: 1Wadsworth Center, New York State Department of Health, Empire State Plaza, Albany, NY, 12201, USA
刊名: Biochemical and Biophysical Research Communications, 2020, Vol.525 (4), pp.1103-1108
来源数据库: Elsevier Journal
DOI: 10.1016/j.bbrc.2020.03.059
关键词: FKBP12Candida aurisCandida glabrataCrystal structureChemical shift perturbationMulti-drug resistance
英文摘要: Abstract(#br)International concern over the recent emergence of Candida auris infections reflects not only its comparative ease of transmission and substantial mortality but the increasing level of resistance observed to all three major classes of antifungal drugs. Diminution in virulence has been reported for a wide range of fungal pathogens when the FK506-binding protein FKBP12 binds to that immunosuppressant drug and the binary complex then inhibits the fungal calcineurin signaling pathway. Structure-based drug design efforts have described modifications of FK506 which modestly reduce virulence for a number of fungal pathogens while also lessening the side effect of suppressing the tissue immunity response in the patient. To aid in such studies, we report the crystal structure of...
全文获取路径: Elsevier  (合作)

  • fungus 真菌
  • Candida 坎迪德
  • protein 蛋白质
  • dimerization 二聚酌
  • pathogenic 病原的
  • transient 瞬变现象
  • auris 
  • structure 构造