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| | <StructureSection load='1xu2' size='340' side='right'caption='[[1xu2]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='1xu2' size='340' side='right'caption='[[1xu2]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1xu2]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XU2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XU2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1xu2]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XU2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1xu1|1xu1]], [[1u5x|1u5x]], [[1u5y|1u5y]], [[1u5z|1u5z]], [[1xut|1xut]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Tnfsf13, APRIL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), TNFRSF17, BCM, BCMA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu2 OCA], [https://pdbe.org/1xu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xu2 RCSB], [https://www.ebi.ac.uk/pdbsum/1xu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xu2 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu2 OCA], [http://pdbe.org/1xu2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xu2 RCSB], [http://www.ebi.ac.uk/pdbsum/1xu2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xu2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Disease == | |
| - | [[http://www.uniprot.org/uniprot/TNR17_HUMAN TNR17_HUMAN]] Note=A chromosomal aberration involving TNFRSF17 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(4;16)(q26;p13) with IL2. | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TNR17_HUMAN TNR17_HUMAN]] Receptor for TNFSF13B/BLyS/BAFF and TNFSF13/APRIL. Promotes B-cell survival and plays a role in the regulation of humoral immunity. Activates NF-kappa-B and JNK.<ref>PMID:10903733</ref> <ref>PMID:10801128</ref> <ref>PMID:10973284</ref> | + | [https://www.uniprot.org/uniprot/TNF13_MOUSE TNF13_MOUSE] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Gordon, N C]] | + | [[Category: Gordon NC]] |
| - | [[Category: Hymowitz, S G]] | + | [[Category: Hymowitz SG]] |
| - | [[Category: Kelley, R F]] | + | [[Category: Kelley RF]] |
| - | [[Category: Pan, B]] | + | [[Category: Pan B]] |
| - | [[Category: Patel, D R]] | + | [[Category: Patel DR]] |
| - | [[Category: Runyon, S]] | + | [[Category: Runyon S]] |
| - | [[Category: Shriver, S K]] | + | [[Category: Shriver SK]] |
| - | [[Category: Skelton, N J]] | + | [[Category: Skelton NJ]] |
| - | [[Category: Starovasnik, M A]] | + | [[Category: Starovasnik MA]] |
| - | [[Category: Wallweber, H J.A]] | + | [[Category: Wallweber HJA]] |
| - | [[Category: Yan, M]] | + | [[Category: Yan M]] |
| - | [[Category: Yin, J]] | + | [[Category: Yin J]] |
| - | [[Category: Crd]]
| + | |
| - | [[Category: Cysteine-rich]]
| + | |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Hormone-growth factor receptor complex]]
| + | |
| - | [[Category: Jelly-roll]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Tnfsf]]
| + | |
| Structural highlights
Function
TNF13_MOUSE
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
TACI is a member of the tumor necrosis factor receptor superfamily and serves as a key regulator of B cell function. TACI binds two ligands, APRIL and BAFF, with high affinity and contains two cysteine-rich domains (CRDs) in its extracellular region; in contrast, BCMA and BR3, the other known high affinity receptors for APRIL and BAFF, respectively, contain only a single or partial CRD. However, another form of TACI exists wherein the N-terminal CRD is removed by alternative splicing. We find that this shorter form is capable of ligand-induced cell signaling and that the second CRD alone (TACI_d2) contains full affinity for both ligands. Furthermore, we report the solution structure and alanine-scanning mutagenesis of TACI_d2 along with co-crystal structures of APRIL.TACI_d2 and APRIL.BCMA complexes that together reveal the mechanism by which TACI engages high affinity ligand binding through a single CRD, and we highlight sources of ligand-receptor specificity within the APRIL/BAFF system.
Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding.,Hymowitz SG, Patel DR, Wallweber HJ, Runyon S, Yan M, Yin J, Shriver SK, Gordon NC, Pan B, Skelton NJ, Kelley RF, Starovasnik MA J Biol Chem. 2005 Feb 25;280(8):7218-27. Epub 2004 Nov 12. PMID:15542592[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hymowitz SG, Patel DR, Wallweber HJ, Runyon S, Yan M, Yin J, Shriver SK, Gordon NC, Pan B, Skelton NJ, Kelley RF, Starovasnik MA. Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high affinity ligand binding. J Biol Chem. 2005 Feb 25;280(8):7218-27. Epub 2004 Nov 12. PMID:15542592 doi:10.1074/jbc.M411714200
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