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| {{STRUCTURE_1oqd| PDB=1oqd | SCENE= }} | | {{STRUCTURE_1oqd| PDB=1oqd | SCENE= }} |
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| '''Crystal structure of sTALL-1 and BCMA'''
| | ===Crystal structure of sTALL-1 and BCMA=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_12721620}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12721620 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12721620}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Zhang, G.]] | | [[Category: Zhang, G.]] |
| [[Category: Ligand receptor complex]] | | [[Category: Ligand receptor complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:09:23 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:22:00 2008'' |
