1oqe

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[[Image:1oqe.gif|left|200px]]<br /><applet load="1oqe" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1oqe.gif|left|200px]]
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caption="1oqe, resolution 2.50&Aring;" />
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'''Crystal structure of sTALL-1 with BAFF-R'''<br />
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{{Structure
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|PDB= 1oqe |SIZE=350|CAPTION= <scene name='initialview01'>1oqe</scene>, resolution 2.50&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal structure of sTALL-1 with BAFF-R'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1OQE is a [[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==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12721620 12721620]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12721620 12721620]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: ligand receptor complex]]
[[Category: ligand receptor complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:20:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:14:11 2008''

Revision as of 11:14, 20 March 2008


PDB ID 1oqe

Drag the structure with the mouse to rotate
, resolution 2.50Å
Coordinates: save as pdb, mmCIF, xml



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

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