Dual specificity protein kinase

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Contents 1 Function 2 Structural highlights 3 3D structures of dual specificity protein kinase 4 References

Function

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.

Structural highlights

The dual specificity protein kinase TTK contains tetratricopeptide repeat domain (TPR) which serves as interaction domain between proteins. The TPR domain is a helical 34 amino acid motif which is found in several copies in a protein which fold together forming a protein-protein binding domain. Cancer therapy potential drugs bind in TTK active site.^[1], ^[2]

3D structures of dual specificity protein kinase

Updated on 03-January-2016

References

1. ↑ 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
2. ↑ Colombo R, Caldarelli M, Mennecozzi M, Giorgini ML, Sola F, Cappella P, Perrera C, Depaolini SR, Rusconi L, Cucchi U, Avanzi N, Bertrand JA, Bossi RT, Pesenti E, Galvani A, Isacchi A, Colotta F, Donati D, Moll J. Targeting the Mitotic Checkpoint for Cancer Therapy with NMS-P715, an Inhibitor of MPS1 Kinase. Cancer Res. 2010 Dec 15;70(24):10255-64. PMID:21159646 doi:10.1158/0008-5472.CAN-10-2101