Structures of human deoxycytidine kinase product complexes.

Publication Type:

Journal Article

Authors:

Soriano, Erika V; Clark, Valerie C; Ealick, Steven E

Source:

Acta Crystallogr D Biol Crystallogr, Volume 63, Issue Pt 12, p.1201-7 (2007)

Keywords:

Crystallography, X-Ray, Deoxycytidine Kinase, Deoxycytidine Monophosphate, Humans, Models, Molecular, Multiprotein Complexes, Protein Conformation, Recombinant Proteins, Structure-Activity Relationship, Substrate Specificity, Uridine Diphosphate

Abstract:

<p>Human deoxycytidine kinase (dCK) is involved in the nucleotide-biosynthesis salvage pathway and has also been shown to phosphorylate several antitumor and antiviral prodrugs. The structures of dCK alone and the dead-end complex of dCK with substrate nucleoside and product ADP or UDP have previously been reported; however, there is currently no structure available for a substrate or product complex. Here, the structures of dCK complexes with the products dCMP, UDP and Mg2+ ion, and with dAMP, UDP and Mg2+ ion are reported. Structural comparisons show that the product complexes with UDP and a dead-end complex with substrate and UDP have similar active-site conformations.</p>

PDB: 
2QRN, 2QRO
Detector: 
Q315
Beamline: 
24-ID-C