Entry | Database: PDB / ID: 6rlc |
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Title | Crystal structure of the PDZ tandem of syntenin in complex with fragment F13 |
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Components | Syntenin-1 |
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Keywords | SIGNALING PROTEIN / signaling protein cell adhesion PDZ domain syntenin syndecan drug design |
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Function / homology | Function and homology information
interleukin-5 receptor complex / interleukin-5 receptor binding / positive regulation of extracellular exosome assembly / syndecan binding / Neurofascin interactions / presynapse assembly / neurexin family protein binding / cytoskeletal anchor activity / substrate-dependent cell migration, cell extension / positive regulation of exosomal secretion ...interleukin-5 receptor complex / interleukin-5 receptor binding / positive regulation of extracellular exosome assembly / syndecan binding / Neurofascin interactions / presynapse assembly / neurexin family protein binding / cytoskeletal anchor activity / substrate-dependent cell migration, cell extension / positive regulation of exosomal secretion / frizzled binding / negative regulation of receptor internalization / protein targeting to membrane / Ephrin signaling / RIPK1-mediated regulated necrosis / positive regulation of transforming growth factor beta receptor signaling pathway / growth factor binding / positive regulation of epithelial to mesenchymal transition / positive regulation of phosphorylation / cell adhesion molecule binding / protein sequestering activity / regulation of mitotic cell cycle / phosphatidylinositol-4,5-bisphosphate binding / ephrin receptor binding / adherens junction / positive regulation of JNK cascade / ionotropic glutamate receptor binding / Regulation of necroptotic cell death / azurophil granule lumen / extracellular vesicle / melanosome / presynapse / actin cytoskeleton organization / positive regulation of cell growth / chemical synaptic transmission / nuclear membrane / Ras protein signal transduction / cytoskeleton / blood microparticle / intracellular signal transduction / positive regulation of cell migration / membrane raft / protein heterodimerization activity / focal adhesion / positive regulation of cell population proliferation / Neutrophil degranulation / protein-containing complex binding / endoplasmic reticulum membrane / negative regulation of transcription by RNA polymerase II / extracellular space / extracellular exosome / extracellular region / nucleoplasm / membrane / identical protein binding / nucleus / plasma membrane / cytoplasm / cytosolSimilarity search - Function |
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Biological species | Homo sapiens (human) |
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Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å |
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Authors | Feracci, M. / Barral, K. |
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Funding support | Belgium, France, 7items Organization | Grant number | Country |
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KU Leuven | GOA/12/016 | Belgium | French National Research Agency | AMIDEX project ANR-11-IDEX-0001-02 | France | Other private | STK-FAF-FA/2016/828 | Belgium | Fondation ARC | ARC PDF20151203700 | France | Fondation ARC | PJA 2016204584 | France | Research Foundation - Flanders | FWO, G.0C57.18N | Belgium | Other private | National League Against Cancer | France |
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Citation | Journal: J Extracell Vesicles / Year: 2020 Title: Pharmacological inhibition of syntenin PDZ2 domain impairs breast cancer cell activities and exosome loadifing with syndecan and EpCAM cargo. Authors: Leblanc, R. / Kashyap, R. / Barral, K. / Egea-Jimenez, A.L. / Kovalskyy, D. / Feracci, M. / Garcia, M. / Derviaux, C. / Betzi, S. / Ghossoub, R. / Platonov, M. / Roche, P. / Morelli, X. / ...Authors: Leblanc, R. / Kashyap, R. / Barral, K. / Egea-Jimenez, A.L. / Kovalskyy, D. / Feracci, M. / Garcia, M. / Derviaux, C. / Betzi, S. / Ghossoub, R. / Platonov, M. / Roche, P. / Morelli, X. / Hoffer, L. / Zimmermann, P. |
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History | Deposition | May 2, 2019 | Deposition site: PDBE / Processing site: PDBE |
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Revision 1.0 | Feb 3, 2021 | Provider: repository / Type: Initial release |
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Revision 1.1 | May 15, 2024 | Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / struct_ncs_dom_lim Item: _citation.country / _database_2.pdbx_DOI ..._citation.country / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id |
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