Mutations Define Cross-talk between the N-terminal Nucleotide-binding Domain and Transmembrane Helix-2 of the Yeast Multidrug Transporter Pdr5: POSSIBLE CONSERVATION OF A SIGNALING INTERFACE FOR COUPLING ATP HYDROLYSIS TO DRUG TRANSPORT

Samankaltaisia teoksia

• An A666G mutation in transmembrane-helix 5 of the yeast multidrug transporter Pdr5 increases drug efflux by enhancing cooperativity between transport sites
  Tekijä: Arya, Nidhi, et al.
  Julkaistu: (2019)
• The Signaling Interface of the Yeast Multidrug Transporter Pdr5 Adopts a Cis Conformation and There Is Functional Overlap and Equivalence of the Deviant and Canonical Q-loop Residues
  Tekijä: Ananthaswamy, Neeti, et al.
  Julkaistu: (2010)
• The multidrug transporter Pdr5 on the 25th anniversary of its discovery: an important model for the study of asymmetric ABC transporters
  Tekijä: Golin, John, et al.
  Julkaistu: (2015)
• Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein
  Tekijä: Sauna, Zuben E., et al.
  Julkaistu: (2000)
• Transport of lipophilic carboxylates is mediated by transmembrane helix 2 in multidrug transporter AcrB
  Tekijä: Oswald, Christine, et al.
  Julkaistu: (2016)