Structural highlights
Function
Q584S0_TRYB2
Publication Abstract from PubMed
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 A 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.
Structures of adenosine kinase from Trypanosoma brucei brucei.,Timm J, Gonzalez-Pacanowska D, Wilson KS Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):34-9. doi:, 10.1107/S2053230X13033621. Epub 2013 Dec 24. PMID:24419613[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Timm J, Gonzalez-Pacanowska D, Wilson KS. Structures of adenosine kinase from Trypanosoma brucei brucei. Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):34-9. doi:, 10.1107/S2053230X13033621. Epub 2013 Dec 24. PMID:24419613 doi:http://dx.doi.org/10.1107/S2053230X13033621