1JH5

Crystal Structure of sTALL-1 of TNF family ligand

Summary for 1JH5

• Entry DOI: 10.2210/pdb1jh5/pdb
• Descriptor: TUMOR NECROSIS FACTOR LIGAND SUPERFAMILY MEMBER 13B (1 entity in total)
• Functional Keywords: tall-1, blys, thank, baff, immune system, antitumor protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 10
• Total formula weight: 162446.02

Authors

Liu, Y.,Xu, L.,Opalka, N.,Shu, H.-B.,Zhang, G. (deposition date: 2001-06-27, release date: 2002-02-08, Last modification date: 2024-02-07)

Primary citation

Liu, Y.,Xu, L.,Opalka, N.,Kappler, J.,Shu, H.B.,Zhang, G.
Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands.
Cell(Cambridge,Mass.), 108:383-394, 2002

PubMed Abstract: 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.

PubMed: 11853672
DOI: 10.1016/S0092-8674(02)00631-1

Experimental method

X-RAY DIFFRACTION (3 Å)