Ligand–receptor binding revealed by the TNF family member TALL-1 (original) (raw)

• Locksley, R. M., Killeen, N. & Lenardo, M. J. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104, 487–501 (2001)
  Article CAS Google Scholar
• Shu, H. B., Hu, W. H. & Johnson, H. TALL-1 is a novel member of the TNF family that is downregulated by mitogens. J. Leukocyte Biol. 65, 680–683 (1999)
  Article CAS Google Scholar
• Schneider, P. et al. BAFF, a novel ligand of the tumour necrosis factor family, stimulates B cell growth. J. Exp. Med. 189, 1747–1756 (1999)
  Article CAS Google Scholar
• Moore, P. A. et al. BlyS: member of the tumour necrosis factor family and B lymphocyte stimulator. Science 285, 260–263 (1999)
  Article CAS Google Scholar
• Mukhopadhyay, A., Ni, J., Zhai, Y., Yu, G. L. & Aggarwal, B. B. Identification and characterization of a novel cytokine, THANK, a TNF homologue that activates apoptosis, nuclear factor-κB, and c-Jun NH2-terminal kinase. J. Biol. Chem. 274, 15978–15981 (1999)
  Article CAS Google Scholar
• Shu, H. B. & Johnson, H. B cell maturation protein is a receptor for the TNF family member TALL-1. Proc. Natl Acad. Sci. USA 97, 9156–9161 (2000)
  Article ADS CAS Google Scholar
• Gross, J. A. et al. TACI and BCMA are receptors for a TNF homologue implicated in B cell autoimmune disease. Nature 404, 995–999 (2000)
  Article ADS CAS Google Scholar
• Thompson, J. S. et al. BAFF binds to the tumour necrosis factor receptor-like molecule B cell maturation antigen and is important for maintaining the peripheral B cell population. J. Exp Med. 192, 129–135 (2000)
  Article CAS Google Scholar
• Marsters, S. A. et al. Interaction of the TNF homologues BLyS and APRIL with the TNF receptor homologues BCMA and TACI. Curr. Biol. 10, 785–788 (2000)
  Article CAS Google Scholar
• Xia, X. Z. et al. TACI is a TRAF-interacting receptor for TALL-1, a tumour necrosis factor family member involved in B cell regulation. J. Exp. Med. 192, 137–143 (2000)
  Article CAS Google Scholar
• Yan, M. et al. Identification of a receptor for BLyS demonstrates a crucial role in humoral immunity. Nature Immunol. 1, 37–41 (2000)
  Article CAS Google Scholar
• Mackay, F. et al. Mice transgenic for BAFF develop lymphocytic disorders along with autoimmune manifestations. J. Exp. Med. 190, 1697–1710 (1999)
  Article CAS Google Scholar
• Khare, S. D. et al. Severe B cell hyperplasia and autoimmune disease in TALL-1 transgenic mice. Proc. Natl Acad. Sci. USA 97, 3370–3375 (2000)
  Article ADS CAS Google Scholar
• Thompson, J. S. et al. BAFF-R, a novel TNF receptor that specifically interacts with BAFF. Science 293, 2108–2111 (2001)
  Article ADS CAS Google Scholar
• Yan, M. et al. Identification of a novel receptor for B lymphocyte stimulator that is mutated in a mouse strain with severe B cell deficiency. Curr. Biol. 11, 1547–1552 (2001)
  Article CAS Google Scholar
• Schiemann, B. et al. An essential role for BAFF in the normal development of B cells through a BCMA-independent pathway. Science 293, 2111–2114 (2001)
  Article ADS CAS Google Scholar
• Gross, J. A. et al. TACI-Ig neutralizes molecules critical for B-cell development and autoimmune disease. Impaired B-cell maturation in mice lacking BlyS. Immunity 15, 289–302 (2001)
  Article CAS Google Scholar
• Xu, S. & Lam, K.-P. B-cell maturation protein, which binds the tumour necrosis factor family members BAFF and APRIL, is dispensable for humoral immune response. Mol. Cell. Biol. 21, 4067–4074 (2001)
  Article CAS Google Scholar
• Von Bulow, G. U., van Deursen, J. M. & Bram, R. J. Regulation of the T-independent humoral response by TACI. Immunity 14, 573–582 (2001)
  Article CAS Google Scholar
• Hahne, M. et al. APRIL, a new ligand of the tumour necrosis factor family, stimulates tumour cell growth. J. Exp. Med. 188, 1185–1190 (1998)
  Article CAS Google Scholar
• Schneider, P. et al. Maturation of marginal zone and follicular B cells requires B cell activation factor of the tumour necrosis factor family and is independent of B cell maturation antigen. J. Exp. Med. 194, 1691–1697 (2001)
  Article CAS Google Scholar
• Mackay, F. & Mackay, C. R. The role of BAFF in B-cell maturation, T-cell activation and autoimmunity. Trends Immunol. 23, 113–115 (2002)
  Article CAS Google Scholar
• Jones, E. Y., Stuart, D. I. & Walker, N. P. Structure of tumour necrosis factor. Nature 338, 225–228 (1989)
  Article ADS CAS Google Scholar
• Eck, M. J. & Sprang, S. R. The structure of tumour necrosis factor-α at 2.6 Å resolution: implications for receptor binding. J. Biol. Chem. 264, 17595–17605 (1989)
  CAS PubMed Google Scholar
• Eck, M. J., Ultsch, M., Rinderknecht, E., de Vos, A. M. & Sprang, S. R. The structure of human lymphotoxin (tumour necrosis factor β) at 1.9 Å resolution. J. Biol. Chem. 267, 2119–2122 (1992)
  CAS PubMed Google Scholar
• Karpusas, M. et al. 2 Å crystal structure of an extracellular fragment of human CD40 ligand. Structure 3, 1031–1039 (1995)
  Article CAS Google Scholar
• Cha, S. S. et al. 2.8 Å resolution crystal structure of human TRAIL, a cytokine with selective antitumor activity. Immunity 11, 253–261 (1999)
  Article CAS Google Scholar
• Lam, J., Nelson, C. A., Ross, F. P., Teitelbaum, S. L. & Fremont, D. H. Crystal structure of the TRANCE/RANKL cytokine reveals determinants of receptor–ligand specificity. J. Clin. Invest. 108, 971–979 (2001)
  Article CAS Google Scholar
• Karpusas, M. et al. Crystal structure of extracellular human BAFF, a TNF family member that stimulates B lymphocytes. J. Mol. Biol. 315, 1145–1154 (2002)
  Article CAS Google Scholar
• Oren, D. A. et al. Structural basis of BlyS receptor recognition. Nature Struct. Biol. 9, 288–292 (2002)
  Article CAS Google Scholar
• Liu, Y. et al. Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands. Cell 108, 383–394 (2002)
  Article CAS Google Scholar
• Banner, D. W. et al. Crystal structure of the soluble human 55 kd TNF receptor–human TNF complex: implications for TNF receptor activation. Cell 73, 431–445 (1993)
  Article CAS Google Scholar
• Mongkolsapaya, J. et al. Structure of the TRAIL–DR5 complex reveals mechanisms conferring specificity in apoptotic initiation. Nature Struct. Biol. 6, 1048–1053 (1999)
  Article CAS Google Scholar
• Hymowitz, S. G. et al. Triggering cell death: the crystal structure of Apo2L/TRAIL in a complex with death receptor 5. Mol. Cell 4, 563–571 (1999)
  Article CAS Google Scholar
• Yu, G. et al. APRIL and TALL-1 and receptors BCMA and TACI: system for regulating humoral immunity. Nature Immunol. 1, 252–256 (2000)
  Article CAS Google Scholar
• Naismith, J. H. & Sprang, S. R. Modularity in the TNF-receptor family. Trends Biochem. Sci. 23, 74–79 (1998)
  Article CAS Google Scholar
• Bodmer, J. L., Schneider, P. & Tschopp, J. The molecular architecture of the TNF superfamily. Trends Biochem. Sci. 27, 19–26 (2002)
  Article CAS Google Scholar
• Kayagaki, N. et al. BAFF/BLyS receptor 3 binds the B cell survival factor BAFF ligand through a discrete surface loop and promotes processing of NF-κB2. Immunity 17, 515–524 (2002)
  Article CAS Google Scholar
• Ware, C. F. APRIL and BAFF connect autoimmunity and cancer. J. Exp. Med. 192, F35–F37 (2000)
  Article CAS Google Scholar
• Brunger, A. T. et al. Crystallography and NMR System (CNS): A new software system for macromolecular structure determination. Acta Crystallogr. D 54, 905–921 (1998)
  Article CAS Google Scholar
• Roschke, V. et al. BlyS and APRIL form biologically active heterotrimers that are expressed in patients with systemic immune-based rheumatic diseases. J. Immunol. 169, 4314–4321 (2002)
  Article CAS Google Scholar
• Otwinowski, Z. & Minor, W. Processing X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307–326 (1997)
  Article CAS Google Scholar
• Jones, T. A., Zou, J.-Y., Cowan, S. & Kjeldgaard, A. L. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A 47, 110–119 (1991)
  Article Google Scholar
• Carson, M. Ribbon models of macromolecules. Methods Enzymol. 277, 493–505 (1997)
  Article CAS Google Scholar
• Esnouf, R. M. BobScript v2.4 changes (C). J. Mol. Graphics 15, 132–134 (1997)
  Article CAS Google Scholar