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    Cell. 2002 Feb 8;108(3):383-94.

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

    Liu Y, Xu L, Opalka N, Kappler J, Shu HB, Zhang G.

    National Jewish Medical and Research Center, Integrated Department of Immunology, Denver, CO 80206, USA.

    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.

    PMID: 11853672 [PubMed - indexed for MEDLINE]

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