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Ligand–receptor binding revealed by the TNF family member TALL-1

Author

Listed:
  • Yingfang Liu
  • Xia Hong
  • John Kappler

    (Howard Hughes Medical Institute
    University of Colorado Health Science Center)

  • Ling Jiang
  • Rongguang Zhang

    (Structural Biology Section, Argonne National Laboratory)

  • Liangguo Xu
  • Cheol-Ho Pan
  • Wesley E. Martin
  • Robert C. Murphy
  • Hong-Bing Shu

    (Peking University)

  • Shaodong Dai
  • Gongyi Zhang

    (Howard Hughes Medical Institute
    University of Colorado Health Science Center)

Abstract

The tumour necrosis factor (TNF) ligand TALL-1 and its cognate receptors, BCMA, TACI and BAFF-R, were recently identified as members of the TNF superfamily, which are essential factors contributing to B-cell maturation. The functional, soluble fragment of TALL-1 (sTALL-1) forms a virus-like assembly for its proper function. Here we determine the crystal structures of sTALL-1 complexed with the extracellular domains of BCMA and BAFF-R at 2.6 and 2.5 Å, respectively. The single cysteine-rich domain of BCMA and BAFF-R both have saddle-like architectures, which sit on the horseback-like surface formed by four coil regions on each individual sTALL-1 monomer. Three novel structural modules, D2, X2 and N, were revealed from the current structures. Sequence alignments, structural modelling and mutagenesis revealed that one disulphide bridge in BAFF-R is critical for determining the binding specificity of the extracellular domain eBAFF-R to TALL-1 instead of APRIL, a closely related ligand of TALL-1, which was confirmed by binding experiments in vitro.

Suggested Citation

  • Yingfang Liu & Xia Hong & John Kappler & Ling Jiang & Rongguang Zhang & Liangguo Xu & Cheol-Ho Pan & Wesley E. Martin & Robert C. Murphy & Hong-Bing Shu & Shaodong Dai & Gongyi Zhang, 2003. "Ligand–receptor binding revealed by the TNF family member TALL-1," Nature, Nature, vol. 423(6935), pages 49-56, May.
    • Handle: RePEc:nat:nature:v:423:y:2003:i:6935:d:10.1038_nature01543
    DOI: 10.1038/nature01543
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