Dual specificity protein kinase

From Proteopedia

Revision as of 19:30, 10 May 2018

spinqualitylabelsall models Dual specificity protein kinase TTK kinase domain complex with inhibitor, 2x9e Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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 or monopolar spindle kinase 1 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 .[1][2]

3D structures of dual specificity protein kinase

Updated on 10-May-2018

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