STK16: Human Serine/Threonine kinase 16
PDB Code: 2BUJ
STK16 (also known as KRCT, Transforming growth factor-beta stimulated factor 1,TGFB stimulated factor 1,TSF1, Protein kinase PKL12, MPSK1, Myristoylated and palmitoylated serine threonine kinase, MPSK) is a protein kinase involved in the control of extracellular matrix-cell adhesion, modulation of focal adhesion structure and the actin cytoskeleton. The protein is ubiquitously expressed with particular high expression in liver, kidney and thymus. Expression of STK16 is enhanced by TGF beta. Over-expression of STK16 leads to disorganization of the Golgi apparatus into vesicular structures, suggesting that STK16 is involved in the secretory pathway. STK16 contains N-terminal recognition sites that may be post translationally modified by myristic acid (glycine 2) and by palmitic acid (cysteine 6 and/or 8).
The protein has been reported to interact with Enolase, N-acetylglucosamine kinase as well as DRG (developmentally regulated GTP-binding protein). ELK1, Histone H1 as well as MBP (Myelin basic protein) have been reported to be recognized as substrates in vitro . STK16 has been also reported to be a sequence specific DNA binding protein that binds to GC-rich elements in vascular endothelial growth factor and type C natriuretic peptide promoters. The DNA binding properties of STK16 are independent its kinase activity.
The structure reported here contains two STK16 monomers in the asymmetric unit. Interestingly, the inhibitor used for co-crystallization (staurosporine) was fond not only in the active site but it mediates also two crystal contacts. The N-terminus forms a beta sheet structure that has not been found in other kinases that have been structure determined so far. The N-terminal sheet mediates a contact with the second STK16 molecule in the asymmetric unit. The most striking feature of the STK16 structure is its unique activation segment that contains a beta sheet structure that is stabilized by a second beta sheet in the C-terminal lobe as well as an alpha helix at the C-terminal end of the activation segment. The surface of the putative substrate binding site is characterized by a strong electrostatic positive potential indicating that substrates recognized by this kinases are rather acidic in nature.
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