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-Structure paper
Title | FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts. |
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Journal, issue, pages | Embo J., Vol. 39, Page e104369-e104369, Year 2020 |
Publish date | Dec 17, 2019 (structure data deposition date) |
Authors | Di Mattia, T. / Martinet, A. / Ikhlef, S. / McEwen, A.G. / Nomine, Y. / Wendling, C. / Poussin-Courmontagne, P. / Voilquin, L. / Eberling, P. / Ruffenach, F. ...Di Mattia, T. / Martinet, A. / Ikhlef, S. / McEwen, A.G. / Nomine, Y. / Wendling, C. / Poussin-Courmontagne, P. / Voilquin, L. / Eberling, P. / Ruffenach, F. / Cavarelli, J. / Slee, J. / Levine, T.P. / Drin, G. / Tomasetto, C. / Alpy, F. |
External links | Embo J. / PubMed:33124732 |
Methods | X-ray diffraction |
Resolution | 1.5 - 2.4 Å |
Structure data | PDB-6tqr: PDB-6tqs: PDB-6tqt: PDB-6tqu: |
Chemicals | ChemComp-CL: ChemComp-HOH: ChemComp-GOL: ChemComp-TFA: ChemComp-SO4: ChemComp-PEG: ChemComp-1PE: ChemComp-EDO: ChemComp-PO4: |
Source |
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Keywords | PROTEIN BINDING / Membrane contact sites / FFAT motif / MSP domain / Endoplasmic reticulum |