An intersubunit lock-and-key ‘Clasp’ motif in the dimer interface of Delta class glutathione transferase

Lignende værker

• Epsilon glutathione transferases possess a unique class-conserved subunit interface motif that directly interacts with glutathione in the active site
  af: Wongsantichon, Jantana, et al.
  Udgivet: (2015)
• Identification, characterization and structure of a new Delta class glutathione transferase isoenzyme
  af: Udomsinprasert, Rungrutai, et al.
  Udgivet: (2005)
• Differences in the subunit interface residues of alternatively spliced glutathione transferases affects catalytic and structural functions
  af: Piromjitpong, Juthamart, et al.
  Udgivet: (2007)
• The intersubunit lock-and-key motif in human glutathione transferase A1-1: role of the key residues Met(51) and Phe(52) in function and dimer stability
  af: Alves, Carla S., et al.
  Udgivet: (2005)
• A sensitive core region in the structure of glutathione S-transferases.
  af: Wongsantichon, Jantana, et al.
  Udgivet: (2003)