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-Structure paper
Title | Structure of human nSMase2 reveals an interdomain allosteric activation mechanism for ceramide generation. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. U.S.A., Vol. 114, Page E5549-E5558, Year 2017 |
Publish date | Feb 20, 2017 (structure data deposition date) |
Authors | Airola, 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 links | Proc. Natl. Acad. Sci. U.S.A. / PubMed:28652336 |
Methods | X-ray diffraction |
Resolution | 1.849 Å |
Structure data | PDB-5uvg: |
Chemicals | ChemComp-CA: ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / sphingomyelinase |