1xu1: Difference between revisions
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==The crystal structure of APRIL bound to TACI== | ==The crystal structure of APRIL bound to TACI== | ||
<StructureSection load='1xu1' size='340' side='right' caption='[[1xu1]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1xu1' size='340' side='right'caption='[[1xu1]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xu1]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1xu1]] 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=1XU1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XU1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xu1 OCA], [https://pdbe.org/1xu1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xu1 RCSB], [https://www.ebi.ac.uk/pdbsum/1xu1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xu1 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [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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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xu/1xu1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xu/1xu1_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 34: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[Tumor necrosis factor ligand superfamily|Tumor necrosis factor ligand superfamily | *[[Tumor necrosis factor ligand superfamily 3D structures|Tumor necrosis factor ligand superfamily 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Gordon | [[Category: Mus musculus]] | ||
[[Category: Hymowitz | [[Category: Gordon NC]] | ||
[[Category: Kelley | [[Category: Hymowitz SG]] | ||
[[Category: Pan | [[Category: Kelley RF]] | ||
[[Category: Patel | [[Category: Pan B]] | ||
[[Category: Runyon | [[Category: Patel DR]] | ||
[[Category: Shriver | [[Category: Runyon S]] | ||
[[Category: Skelton | [[Category: Shriver SK]] | ||
[[Category: Starovasnik | [[Category: Skelton NJ]] | ||
[[Category: Wallweber | [[Category: Starovasnik MA]] | ||
[[Category: Yan | [[Category: Wallweber HJA]] | ||
[[Category: Yin | [[Category: Yan M]] | ||
[[Category: Yin J]] | |||
Latest revision as of 03:40, 21 November 2024
The crystal structure of APRIL bound to TACIThe crystal structure of APRIL bound to TACI
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedTACI 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 AlsoReferences
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