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Dual specificity protein kinase
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(Difference between revisions)
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{{STRUCTURE_2x9e| PDB=2x9e | SIZE=400| SCENE= |right|CAPTION=Dual specificity protein kinase TTK kinase domain complex with inhibitor, [[2x9e]] }} | {{STRUCTURE_2x9e| PDB=2x9e | SIZE=400| SCENE= |right|CAPTION=Dual specificity protein kinase TTK kinase domain complex with inhibitor, [[2x9e]] }} | ||
| - | '''Dual specificity protein kinases''' are kinases which act as both tyrosine kinase and serine/threonine kinase. CLK1 phosphorylates serine/arginine-rich proteins involved in pre-mRNA processing. The dual specificity protein kinase TTK contains tetra-trico-peptide repeat domain (TPR) which serves as interaction domain between proteins. | + | '''Dual specificity protein kinases''' are kinases which act as both tyrosine kinase and serine/threonine kinase. '''CLK1''' phosphorylates serine/arginine-rich proteins involved in pre-mRNA processing. The dual specificity protein kinase '''TTK''' contains tetra-trico-peptide repeat domain (TPR) which serves as interaction domain between proteins.<ref>PMID:9779990</ref> |
==3D structures of dual specificity protein kinase== | ==3D structures of dual specificity protein kinase== | ||
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**[[3hmp]] - hTTK kinase domain + quinazolin ligand | **[[3hmp]] - hTTK kinase domain + quinazolin ligand | ||
}} | }} | ||
| + | == References == | ||
| + | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 15:13, 3 January 2016
Dual specificity protein kinases are kinases which act as both tyrosine kinase and serine/threonine kinase. CLK1 phosphorylates serine/arginine-rich proteins involved in pre-mRNA processing. The dual specificity protein kinase TTK contains tetra-trico-peptide repeat domain (TPR) which serves as interaction domain between proteins.[1]
3D structures of dual specificity protein kinase
Updated on 03-January-2016
References
- ↑ Dhanasekaran N, Premkumar Reddy E. Signaling by dual specificity kinases. Oncogene. 1998 Sep 17;17(11 Reviews):1447-55. PMID:9779990 doi:http://dx.doi.org/10.1038/sj.onc.1202251
