Crystal structure of the Leishmania major MIX protein: A scaffold protein that mediates protein-protein interactions
Michael A Gorman, Alex D Uboldi, Peter J Walsh, Kher Shing Tan, Guido Hansen, Trevor Huyton, Hong Ji, Joan Curtis, Lukasz Kedzierski, Anthony T Papenfuss, Con Dogovski, Matthew A Perugini, Richard J Simpson, Emanuela Handman, Michael W Parker
Protein Science | WILEY | Published : 2011
Infection by Leishmania and Trypanosoma causes severe disease and can be fatal. The reduced effectiveness of current treatments is largely due to drug resistance, hence the urgent need to develop new drugs, preferably against novel targets. We have recently identified a mitochondrial membrane-anchored protein, designated MIX, which occurs exclusively in these parasites and is essential for virulence. We have determined the crystal structure of Leishmania major MIX to a resolution of 2.4 Å. MIX forms an all α-helical fold comprising seven α-helices that fold into a single domain. The distribution of helices is similar to a number of scaffold proteins, namely HEAT repeats, 14-3-3, and tetratri..View full abstract
Awarded by Australian National Health and Medical Research Council
Grant sponsor: Australian National Health and Medical Research Council Program; Grant numbers: 487922; 406601; Grant sponsor: Australian Research Council Federation Fellowship and Future Fellowship.