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TitleStructure of human nSMase2 reveals an interdomain allosteric activation mechanism for ceramide generation.
Journal, issue, pagesProc. Natl. Acad. Sci. U.S.A., Vol. 114, Page E5549-E5558, Year 2017
Publish dateFeb 20, 2017 (structure data deposition date)
AuthorsAirola, M.V. / Shanbhogue, P. / Shamseddine, A.A. / Guja, K.E. / Senkal, C.E. / Maini, R. / Bartke, N. / Wu, B.X. / Obeid, L.M. / Garcia-Diaz, M. / Hannun, Y.A.
External linksProc. Natl. Acad. Sci. U.S.A. / PubMed:28652336
MethodsX-ray diffraction
Resolution1.849 Å
Structure data

PDB-5uvg:
Crystal structure of the human neutral sphingomyelinase 2 (nSMase2) catalytic domain with insertion deleted and calcium bound
Method: X-RAY DIFFRACTION / Resolution: 1.849 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / sphingomyelinase

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