5FTU
Tetrameric complex of Latrophilin 3, Unc5D and FLRT2
Summary for 5FTU
| Entry DOI | 10.2210/pdb5ftu/pdb |
| Related | 5FTT |
| Descriptor | NETRIN RECEPTOR UNC5D, LEUCINE-RICH REPEAT TRANSMEMBRANE PROTEIN FLRT2, ADHESION G PROTEIN-COUPLED RECEPTOR L3, ... (6 entities in total) |
| Functional Keywords | signaling protein, signalling protein, leucine-rich repeat, lrr, unc5, apoptosis, uncoordinated-5, netrin receptor, flrt, latrophilin, adhesion, repulsion, guidance, beta propellor, immunoglobulin, thrombospondin, olfactomedin, lectin, tetramer |
| Biological source | RATTUS NORVEGICUS (NORWAY RAT) More |
| Total number of polymer chains | 12 |
| Total formula weight | 428824.55 |
| Authors | Jackson, V.A.,Mehmood, S.,Chavent, M.,Roversi, P.,Carrasquero, M.,del Toro, D.,Seyit-Bremer, G.,Ranaivoson, F.M.,Comoletti, D.,Sansom, M.S.P.,Robinson, C.V.,Klein, R.,Seiradake, E. (deposition date: 2016-01-15, release date: 2016-05-04, Last modification date: 2024-01-10) |
| Primary citation | Jackson, V.A.,Mehmood, S.,Chavent, M.,Roversi, P.,Carrasquero, M.,Del Toro, D.,Seyit-Bremer, G.,Ranaivoson, F.M.,Comoletti, D.,Sansom, M.S.P.,Robinson, C.V.,Klein, R.,Seiradake, E. Super-Complexes of Adhesion Gpcrs and Neural Guidance Receptors Nat.Commun., 7:11184-, 2016 Cited by PubMed Abstract: Latrophilin adhesion-GPCRs (Lphn1-3 or ADGRL1-3) and Unc5 cell guidance receptors (Unc5A-D) interact with FLRT proteins (FLRT1-3), thereby promoting cell adhesion and repulsion, respectively. How the three proteins interact and function simultaneously is poorly understood. We show that Unc5D interacts with FLRT2 in cis, controlling cell adhesion in response to externally presented Lphn3. The ectodomains of the three proteins bind cooperatively. Crystal structures of the ternary complex formed by the extracellular domains reveal that Lphn3 dimerizes when bound to FLRT2:Unc5, resulting in a stoichiometry of 1:1:2 (FLRT2:Unc5D:Lphn3). This 1:1:2 complex further dimerizes to form a larger 'super-complex' (2:2:4), using a previously undescribed binding motif in the Unc5D TSP1 domain. Molecular dynamics simulations, point-directed mutagenesis and mass spectrometry demonstrate the stability and molecular properties of these complexes. Our data exemplify how receptors increase their functional repertoire by forming different context-dependent higher-order complexes. PubMed: 27091502DOI: 10.1038/NCOMMS11184 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (6.01 Å) |
Structure validation
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