Structure of Human Acid Sphingomyelinase Reveals the Role of the Saposin Domain in Activating Substrate Hydrolysis
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- 作者：Zi-Jian Xiong1 ; Jingjing Huang1 ; Gennady Poda2 ; 3 ; Ré ; gis Pomè ; s1 ; 4 ; Gilbert G. Privé ; 1 ; 5 ; 6 ; prive@uhnres.utoronto.ca" class="auth_mail" title="E-mail the corresponding author
- 关键词：ASM ; acid sphingomyelinase ; Sap ; sphingolipid activator protein ; NPD ; Niemann-Pick Disease ; SM ; sphingomyelin ; Chol ; cholesterol ; PC ; phosphatidylcholine ; PG ; phosphatidylglycerol ; POPG ; 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol ; BMP ; bis(monoacylglycero)phosphate ; MD ; molecular dynamics ; CG ; coarse grained
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：31 July 2016
- 年：2016
- 卷：428
- 期：15
- 页码：3026-3042
- 全文大小：2979 K
文摘
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Crystal structure of human acid sphingomyelinase (ASM).
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10">The ASM saposin domain and connector regions are tightly associated with the metallophosphatase catalytic domain.
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15">The saposin domain undergoes hinge-opening and maintains its association with the catalytic domain upon membrane binding.
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20">Membrane binding by the saposin domain guides the active site of the catalytic domain to the headgroups of the bilayer.
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25">The model for ASM membrane binding provides structural insight into saposin-hydrolase complexes at bilayer surfaces.