Structures of adenosine kinase from Trypanosoma brucei brucei

Jennifer Timm, Dolores González-Pacanowska, Keith S. Wilson*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Trypanosoma brucei is a single-cellular parasite of the genus Kinetoplastida and is the causative agent of African sleeping sickness in humans. Adenosine kinase is a key enzyme in the purine-salvage pathway, phosphorylating adenosine to AMP, and also activates cytotoxic analogues such as cordycepin and Ara-A by their phosphorylation. The structures of T. brucei brucei adenosine kinase (TbAK) in its unliganded open conformation and complexed with adenosine and ADP in the closed conformation are both reported to 2.6 Å resolution. The structures give insight into the binding mode of the substrates and the conformational change induced upon substrate binding. This information can be used to guide the improvement of cytotoxic substrate analogues as potential antitrypanosomal drugs.

Original languageEnglish
Pages (from-to)34-39
Number of pages6
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number1
Publication statusPublished - Jan 2014


  • adenosine kinase
  • ligand complex
  • Trypanosoma brucei brucei

Cite this