Plasmodium falciparum putative endoplasmin homolog precursor (PFL1070c), in complex with a a thienopyrimidine derivative

Target ID:

PP-HSP90

Deposition Date:

Tuesday 26th October 2010

Families:

Miscellaneous

Related Diseases:

Parasitic disease

Structure type:

protein-ligand

Download Coordinates:

3PEH

Authors:

Wernimont AK, Hutchinson A, Weadge J, Cossar, D., MacKenzie F, Vedadi M, Senisterra G, Arrowsmith CH, Edwards AM, Bountra C, Weigelt J, Wyatt PG, Fairlamb AH, MacKenzie C, Ferguson MAJ, Hui R, Pizarro JC, Hills T

Site:

Toronto

3PEH

tabs

Structure Details

HSP90 is a chaperone protein implicated in protein folding, stress response and protein degradation. The malaria parasite Plasmodium falciparum contains 4 HSP90 paralogs, including HSP90, TRAP1 and GRP94. We present herein the structure of the N-terminal domain of PfGRP94 with thienopyrimidine bound. We have also solved the structures of other parasite HSP90s bound with inhibitors, including PfGRP94 with macbecin (3PEJ), Leishmania HSP90 with DMAP (3Q5J), Leishmania HSP90 with DDU101323 (3Q5K) and Leishmania HSP90 with AEP (3Q5L).