1OQE

Crystal structure of sTALL-1 with BAFF-R

Summary for 1OQE

• Entry DOI: 10.2210/pdb1oqe/pdb
• Related: 1JH5 1OQD
• Descriptor: Tumor necrosis factor ligand superfamily member 13B, soluble form, Tumor necrosis factor receptor superfamily member 13C (2 entities in total)
• Functional Keywords: ligand receptor complex, immune system
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type II membrane protein. Tumor necrosis factor ligand superfamily member 13b, soluble form: Secreted: Q9Y275; Membrane ; Single-pass type III membrane protein : Q96RJ3
• Total number of polymer chains: 18
• Total formula weight: 189374.61

Authors

Zhang, G. (deposition date: 2003-03-07, release date: 2003-05-13, Last modification date: 2024-11-13)

Primary citation

Liu, Y.,Hong, X.,Kappler, J.,Jiang, L.,Zhang, R.,Xu, L.,Pan, C.H.,Martin, W.E.,Murphy, R.C.,Shu, H.B.,Dai, S.,Zhang, G.
Ligand-receptor binding revealed by the TNF family member TALL-1.
Nature, 423:49-56, 2003

PubMed 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 A, 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.

PubMed: 12721620
DOI: 10.1038/nature01543

Experimental method

X-RAY DIFFRACTION (2.5 Å)