1OQD

Crystal structure of sTALL-1 and BCMA

1OQD の概要

• エントリーDOI: 10.2210/pdb1oqd/pdb
• 関連するPDBエントリー: 1JH5 1OQE
• 分子名称: Tumor necrosis factor ligand superfamily member 13B, soluble form, Tumor necrosis factor receptor superfamily member 17 (2 entities in total)
• 機能のキーワード: ligand receptor complex, immune response
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cell membrane; Single-pass type II membrane protein. Tumor necrosis factor ligand superfamily member 13b, soluble form: Secreted: Q9Y275; Cell membrane; Single-pass type III membrane protein: Q02223
• タンパク質・核酸の鎖数: 18
• 化学式量合計: 197413.57

構造登録者

Zhang, G. (登録日: 2003-03-07, 公開日: 2003-05-13, 最終更新日: 2024-11-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.6 Å)