6TQS
The crystal structure of the MSP domain of human MOSPD2 in complex with the conventional FFAT motif of ORP1.
Summary for 6TQS
Entry DOI | 10.2210/pdb6tqs/pdb |
Descriptor | Motile sperm domain-containing protein 2, Oxysterol-binding protein-related protein 1, GLYCEROL, ... (9 entities in total) |
Functional Keywords | membrane contact sites, ffat motif, msp domain, endoplasmic reticulum, protein binding |
Biological source | Homo sapiens (Human) More |
Total number of polymer chains | 11 |
Total formula weight | 159233.47 |
Authors | McEwen, A.G.,Poussin-Courmontagne, P.,Di Mattia, T.,Wendling, C.,Cavarelli, J.,Tomasetto, C.,Alpy, F. (deposition date: 2019-12-17, release date: 2020-11-18, Last modification date: 2024-01-24) |
Primary citation | 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. FFAT motif phosphorylation controls formation and lipid transfer function of inter-organelle contacts. Embo J., 39:e104369-e104369, 2020 Cited by PubMed: 33124732DOI: 10.15252/embj.2019104369 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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