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Molecular basis for the catalytic mechanism of human neutral sphingomyelinases 1 (hSMPD2)

Nat Commun. 2023-11; 
Jingbo Yi, Boya Qi, Jian Yin, Ruochong Li, Xudong Chen, Junhan Hu, Guohui Li, Sensen Zhang, Yuebin Zhang, Maojun Yang
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Proteins, Expression, Isolation and Analysis … For Western blot analysis, proteins were subjected to a 4 to 20% SDS–polyacrylamide gel electrophoresis gel (GenScript) and transferred onto a polyvinylidene difluoride membrane (… Get A Quote

摘要

Enzymatic breakdown of sphingomyelin by sphingomyelinase (SMase) is the main source of the membrane lipids, ceramides, which are involved in many cellular physiological processes. However, the full-length structure of human neutral SMase has not been resolved; therefore, its catalytic mechanism remains unknown. Here, we resolve the structure of human full-length neutral SMase, sphingomyelinase 1 (SMPD2), which reveals that C-terminal transmembrane helices contribute to dimeric architecture of hSMPD2 and that D111?-?K116 loop domain is essential for substrate hydrolysis. Coupled with molecular docking, we clarify the binding pose of sphingomyelin, and site-directed mutagenesis further confirms key residues r... More

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