1oqe
From Proteopedia
(New page: 200px<br /> <applet load="1oqe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oqe, resolution 2.50Å" /> '''Crystal structure o...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1oqe.gif|left|200px]]<br /> | + | [[Image:1oqe.gif|left|200px]]<br /><applet load="1oqe" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1oqe" size=" | + | |
caption="1oqe, resolution 2.50Å" /> | caption="1oqe, resolution 2.50Å" /> | ||
'''Crystal structure of sTALL-1 with BAFF-R'''<br /> | '''Crystal structure of sTALL-1 with BAFF-R'''<br /> | ||
==Overview== | ==Overview== | ||
| - | 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 | + | 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 Structure== | ==About this Structure== | ||
| - | 1OQE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1OQE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OQE OCA]. |
==Reference== | ==Reference== | ||
| Line 17: | Line 16: | ||
[[Category: ligand receptor complex]] | [[Category: ligand receptor complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:25 2008'' |
Revision as of 12:20, 21 February 2008
|
Crystal structure of sTALL-1 with BAFF-R
Overview
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 Structure
1OQE is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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 Thu Feb 21 14:20:25 2008
