Thymidine kinase
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | <StructureSection load='2j9r' size='450' side='right' caption='Thymidine kinase complex with thymidine | + | <StructureSection load='2j9r' size='450' side='right' caption='Thymidine kinase complex with thymidine, phosphate and Zn+2 ion (grey) (PDB entry [[2j94]])' scene='45/455455/Cv/1'> |
== Function == | == Function == | ||
'''Thymidine kinase''' (TK) catalyzes the conversion of deoxythymidine (THM) to deoxythymidine 5’-phosphate (THMP) with the conversion of ATP to ADP. TK has an important role in the synthesis of DNA. It is required for the action of many antiviral drugs. Higher organisms have 2 isozymes. '''TK1''' is cell cycle-dependent while '''TK2''' <ref>PMID:18459168</ref>is found in the mitochondria and is cell cycle-independent. TK undergoes feed-back regulation by thymidine triphosphate (TTP). Adenosyl-thymidyl-tetraphosphate (TP4A) is a bisubstrate inhibitor of TK. For more details see [[Herpes Simplex Virus Thymidine Kinase]]. | '''Thymidine kinase''' (TK) catalyzes the conversion of deoxythymidine (THM) to deoxythymidine 5’-phosphate (THMP) with the conversion of ATP to ADP. TK has an important role in the synthesis of DNA. It is required for the action of many antiviral drugs. Higher organisms have 2 isozymes. '''TK1''' is cell cycle-dependent while '''TK2''' <ref>PMID:18459168</ref>is found in the mitochondria and is cell cycle-independent. TK undergoes feed-back regulation by thymidine triphosphate (TTP). Adenosyl-thymidyl-tetraphosphate (TP4A) is a bisubstrate inhibitor of TK. For more details see [[Herpes Simplex Virus Thymidine Kinase]]. | ||
| Line 10: | Line 10: | ||
== Structural highlights == | == Structural highlights == | ||
| - | Thymidine and phosphate are bound in the hydrophobic active site pocket of TK<ref>PMID:17288553</ref>. | + | The biological assembly of Thymidine kinase is <scene name='45/455455/Cv/3'>homotetramer</scene>. Thymidine and phosphate are bound in the hydrophobic active site pocket of TK<ref>PMID:17288553</ref>. |
</StructureSection> | </StructureSection> | ||
Revision as of 07:04, 18 September 2016
| |||||||||||
3D Structures of thymidine kinase
Updated on 18-September-2016
References
- ↑ Perez-Perez MJ, Priego EM, Hernandez AI, Familiar O, Camarasa MJ, Negri A, Gago F, Balzarini J. Structure, physiological role, and specific inhibitors of human thymidine kinase 2 (TK2): present and future. Med Res Rev. 2008 Sep;28(5):797-820. doi: 10.1002/med.20124. PMID:18459168 doi:http://dx.doi.org/10.1002/med.20124
- ↑ He Q, Zhang P, Zou L, Li H, Wang X, Zhou S, Fornander T, Skog S. Concentration of thymidine kinase 1 in serum (S-TK1) is a more sensitive proliferation marker in human solid tumors than its activity. Oncol Rep. 2005 Oct;14(4):1013-9. PMID:16142366
- ↑ Saada A, Shaag A, Mandel H, Nevo Y, Eriksson S, Elpeleg O. Mutant mitochondrial thymidine kinase in mitochondrial DNA depletion myopathy. Nat Genet. 2001 Nov;29(3):342-4. PMID:11687801 doi:http://dx.doi.org/10.1038/ng751
- ↑ Kosinska U, Carnrot C, Sandrini MP, Clausen AR, Wang L, Piskur J, Eriksson S, Eklund H. Structural studies of thymidine kinases from Bacillus anthracis and Bacillus cereus provide insights into quaternary structure and conformational changes upon substrate binding. FEBS J. 2007 Feb;274(3):727-37. PMID:17288553 doi:10.1111/j.1742-4658.2006.05617.x
