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- W2170400518 abstract "Sphingosine kinase 1 (SphK1) is a lipid kinase that catalyzes the conversion of sphingosine to sphingosine-1-phosphate (S1P), which has been shown to play a role in lymphocyte trafficking, angiogenesis, and response to apoptotic stimuli. As a central enzyme in modulating the S1P levels in cells, SphK1 emerges as an important regulator for diverse cellular functions and a potential target for drug discovery. Here, we present the crystal structures of human SphK1 in the apo form and in complexes with a substrate sphingosine-like lipid, ADP, and an inhibitor at 2.0-2.3 Å resolution. The SphK1 structures reveal a two-domain architecture in which its catalytic site is located in the cleft between the two domains and a hydrophobic lipid-binding pocket is buried in the C-terminal domain. Comparative analysis of these structures with mutagenesis and kinetic studies provides insight into how SphK1 recognizes the lipid substrate and catalyzes ATP-dependent phosphorylation." @default.
- W2170400518 created "2016-06-24" @default.
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- W2170400518 creator A5086008939 @default.
- W2170400518 date "2013-05-01" @default.
- W2170400518 modified "2023-10-12" @default.
- W2170400518 title "Molecular Basis of Sphingosine Kinase 1 Substrate Recognition and Catalysis" @default.
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- W2170400518 doi "https://doi.org/10.1016/j.str.2013.02.025" @default.
- W2170400518 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23602659" @default.
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