Summary for 4EN0
| Entry DOI | 10.2210/pdb4en0/pdb |
| Descriptor | Tumor necrosis factor ligand superfamily member 14, PHOSPHATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | structural genomics, psi-biology, new york structural genomics research consortium, nysgrc, immunity, tnf superfamily, hvem, dcr3, n-glycosylation, membrane, secreted protein, cytokine, atoms-to-animals: the immune function network, ifn, jelly-roll fold, bind tnf receptor hvem and ltbr, ltbr |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 3 |
| Total formula weight | 55706.73 |
| Authors | Zhan, C.,Liu, W.,Patskovsky, Y.,Ramagopal, U.A.,Bonanno, J.B.,Nathenson, S.G.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC),Atoms-to-Animals: The Immune Function Network (IFN) (deposition date: 2012-04-12, release date: 2012-05-09, Last modification date: 2024-11-20) |
| Primary citation | Liu, W.,Zhan, C.,Cheng, H.,Kumar, P.R.,Bonanno, J.B.,Nathenson, S.G.,Almo, S.C. Mechanistic basis for functional promiscuity in the TNF and TNF receptor superfamilies: structure of the LIGHT:DcR3 assembly. Structure, 22:1252-1262, 2014 Cited by PubMed Abstract: LIGHT initiates intracellular signaling via engagement of the two TNF receptors, HVEM and LTβR. In humans, LIGHT is neutralized by DcR3, a unique soluble member of the TNFR superfamily, which tightly binds LIGHT and inhibits its interactions with HVEM and LTβR. DcR3 also neutralizes two other TNF ligands, FasL and TL1A. Due to its ability to neutralize three distinct different ligands, DcR3 contributes to a wide range of biological and pathological processes, including cancer and autoimmune diseases. However, the mechanisms that support the broad specificity of DcR3 remain to be fully defined. We report the structures of LIGHT and the LIGHT:DcR3 complex, which reveal the structural basis for the DcR3-mediated neutralization of LIGHT and afford insights into DcR3 function and binding promiscuity. Based on these structures, we designed LIGHT mutants with altered affinities for DcR3 and HVEM, which may represent mechanistically informative probe reagents. PubMed: 25087510DOI: 10.1016/j.str.2014.06.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
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