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.
journal_name
Naturejournal_title
Natureauthors
Liu Y,Hong X,Kappler J,Jiang L,Zhang R,Xu L,Pan CH,Martin WE,Murphy RC,Shu HB,Dai S,Zhang Gdoi
10.1038/nature01543keywords:
subject
Has Abstractpub_date
2003-05-01 00:00:00pages
49-56issue
6935eissn
0028-0836issn
1476-4687pii
nature01543journal_volume
423pub_type
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