1XU2
The crystal structure of APRIL bound to BCMA
Summary for 1XU2
| Entry DOI | 10.2210/pdb1xu2/pdb |
| Related | 1U5X 1U5Y 1U5Z 1XU1 1XUT |
| Descriptor | Tumor necrosis factor ligand superfamily member 13, Tumor necrosis factor receptor superfamily member 17, NICKEL (II) ION, ... (4 entities in total) |
| Functional Keywords | tnfsf, cytokine, crd, receptor, jelly-roll, cysteine-rich, hormone-growth factor receptor complex, hormone/growth factor receptor |
| Biological source | Mus musculus (house mouse) More |
| Cellular location | Secreted (By similarity): Q9D777 Cell membrane; Single-pass type III membrane protein: Q02223 |
| Total number of polymer chains | 6 |
| Total formula weight | 62082.66 |
| Authors | Hymowitz, S.G.,Patel, D.R.,Wallweber, H.J.A.,Runyon, S.,Yan, M.,Yin, J.,Shriver, S.K.,Gordon, N.C.,Pan, B.,Skelton, N.J.,Kelley, R.F.,Starovasnik, M.A. (deposition date: 2004-10-25, release date: 2004-11-09, Last modification date: 2024-10-16) |
| Primary citation | Hymowitz, S.G.,Patel, D.R.,Wallweber, H.J.A.,Runyon, S.,Yan, M.,Yin, J.,Shriver, S.K.,Gordon, N.C.,Pan, B.,Skelton, N.J.,Kelley, R.F.,Starovasnik, M.A. Structures of APRIL-receptor complexes: Like BCMA, TACI employs only a single cysteine-rich domain for high-affinity ligand binding J.Biol.Chem., 280:7218-7227, 2005 Cited by PubMed Abstract: TACI is a member of the tumor necrosis factor receptor superfamily and serves as a key regulator of B cell function. TACI binds two ligands, APRIL and BAFF, with high affinity and contains two cysteine-rich domains (CRDs) in its extracellular region; in contrast, BCMA and BR3, the other known high affinity receptors for APRIL and BAFF, respectively, contain only a single or partial CRD. However, another form of TACI exists wherein the N-terminal CRD is removed by alternative splicing. We find that this shorter form is capable of ligand-induced cell signaling and that the second CRD alone (TACI_d2) contains full affinity for both ligands. Furthermore, we report the solution structure and alanine-scanning mutagenesis of TACI_d2 along with co-crystal structures of APRIL.TACI_d2 and APRIL.BCMA complexes that together reveal the mechanism by which TACI engages high affinity ligand binding through a single CRD, and we highlight sources of ligand-receptor specificity within the APRIL/BAFF system. PubMed: 15542592DOI: 10.1074/jbc.M411714200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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