Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands

Cell. 2002 Feb 8;108(3):383-94. doi: 10.1016/s0092-8674(02)00631-1.


TALL-1/BAFF/BLyS was recently identified as a member of the tumor necrosis factor (TNF) ligand family. The crystal structure of the functional soluble TALL-1 (sTALL-1) has been determined at 3.0 A. sTALL-1 forms a virus-like assembly with 200 A diameter in the crystals, containing 60 sTALL-1 monomers. The cluster formation is mediated by a "flap" region of the sTALL-1 monomer. The virus-like assembly was also detected in solution using gel filtration and electron microscopy. Deletion of the flap region disrupted the formation of the virus-like assembly. The mutant sTALL-1 still bound its receptor but could not activate NF-kappaB and did not stimulate B lymphocyte proliferation. Finally, we found the virus-like cluster of sTALL-1 exists in physiological condition. We propose that this virus-like assembly of sTALL-1 is the functional unit for TALL-1 in vivo.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • B-Cell Activating Factor
  • Humans
  • Membrane Proteins / chemistry*
  • Membrane Proteins / metabolism
  • Membrane Proteins / ultrastructure
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Binding
  • Protein Conformation
  • Receptors, Tumor Necrosis Factor / metabolism
  • Structure-Activity Relationship
  • Tumor Necrosis Factor-alpha / chemistry*
  • Tumor Necrosis Factor-alpha / metabolism
  • Tumor Necrosis Factor-alpha / ultrastructure
  • Virus Assembly


  • B-Cell Activating Factor
  • Membrane Proteins
  • Receptors, Tumor Necrosis Factor
  • TNFSF13B protein, human
  • Tumor Necrosis Factor-alpha

Associated data

  • PDB/1JH5