1oqd: Difference between revisions
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'''Crystal structure of sTALL-1 and BCMA''' | '''Crystal structure of sTALL-1 and BCMA''' | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Zhang, G.]] | [[Category: Zhang, G.]] | ||
[[Category: | [[Category: Ligand receptor complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:09:23 2008'' | |||
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Revision as of 04:09, 3 May 2008
Crystal structure of sTALL-1 and BCMA
OverviewOverview
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.
About this StructureAbout this Structure
1OQD is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Ligand-receptor binding revealed by the TNF family member TALL-1., Liu Y, Hong X, Kappler J, Jiang L, Zhang R, Xu L, Pan CH, Martin WE, Murphy RC, Shu HB, Dai S, Zhang G, Nature. 2003 May 1;423(6935):49-56. PMID:12721620 Page seeded by OCA on Sat May 3 04:09:23 2008