Ser-241位于子结构域VII和VIII之间的PDK1激酶结构域的激活环中，其位置与PDK1在其蛋白激酶底物上磷酸化的位点相同。 细菌中表达的PDK1活跃并在Ser-241处被磷酸化，

Phospho-PDK1 (Ser241) Antibody detects PDK1 only when phosphorylated at Ser241. Human, Mouse, Rat. Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser241 of human PDK1. Antibodies are purified by protein A and peptide affinity chromatography.

1999年9月9日 · 3-phosphoinositide-dependent protein kinase-1 (PDK1) expressed in unstimulated 293 cells was phosphorylated at Ser-25, Ser-241, Ser-393, Ser-396 and Ser-410 and the level of phosphorylation of each site was unaffected by …

In this study we have demonstrated by mutational analysis that interactions between the phosphorylated Ser-241 and the αC-helix are not required for PDK1 activity or substrate binding through the HM-pocket but are necessary for PDK1 to be activated or stabilized by a peptide that binds to this site.

2018年2月1日 · An increasing amount of evidence hints at 3-phosphoinositide dependent protein kinase-1 (PDK1 or PDPK1) as an intriguing and underexplored target for cancer therapy. Several reports show that PDK1 expression is dysregulated in multiple cancer types.

2022年4月6日 · PDK1 (3-phosphoinositide-dependent kinase 1) is a serine/threonine-protein kinase that plays a central role in regulating cell growth, survival, and proliferation. Knocking out PDK1 in mice...

3-Phosphoinositide–dependent kinase 1 (PDK1) plays a central role in regulating the activity of protein kinases that are essential for signaling; however, how PDK1 itself is regulated is largely unknown. We found that homodimerization of PDK1 is a spatially and temporally regulated mechanism for controlling PDK1 activity.

1999年9月1日 · 3-phosphoinositide-dependent protein kinase-1 (PDK1) expressed in unstimulated 293 cells was phosphorylated at Ser-25, Ser-241, Ser-393, Ser-396 and Ser-410 and the level of phosphorylation of each site was unaffected by …

The Ser-241 phosphorylated form is distributed along the perinuclear region in neuronal cells while in non-neuronal cells it is found in both the nucleus and the cytoplasm. IGF1 transiently increases phosphorylation at Ser-241 of neuronal PDPK1, resulting in its translocation to other cellular compartments.

2005年1月26日 · This structure, together with surface plasmon resonance binding studies, demonstrates that the PDK1 (S241A)-inactive mutant possesses an intact HM-pocket as well as an ordered alpha C-helix. These findings reveal that the integrity of the alpha C-helix and HM-pocket in PDK1 is not regulated by T-loop phosphorylation.