1jh5: Difference between revisions
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==Crystal Structure of sTALL-1 of TNF family ligand== | ==Crystal Structure of sTALL-1 of TNF family ligand== | ||
<StructureSection load='1jh5' size='340' side='right' caption='[[1jh5]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1jh5' size='340' side='right' caption='[[1jh5]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jh5]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JH5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jh5]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JH5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JH5 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jh5 OCA], [http://pdbe.org/1jh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jh5 RCSB], [http://www.ebi.ac.uk/pdbsum/1jh5 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jh5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jh5 OCA], [http://pdbe.org/1jh5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jh5 RCSB], [http://www.ebi.ac.uk/pdbsum/1jh5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jh5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/1jh5_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jh/1jh5_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
Revision as of 12:22, 17 January 2018
Crystal Structure of sTALL-1 of TNF family ligandCrystal Structure of sTALL-1 of TNF family ligand
Structural highlights
Function[TN13B_HUMAN] Cytokine that binds to TNFRSF13B/TACI and TNFRSF17/BCMA. TNFSF13/APRIL binds to the same 2 receptors. Together, they form a 2 ligands -2 receptors pathway involved in the stimulation of B- and T-cell function and the regulation of humoral immunity. A third B-cell specific BAFF-receptor (BAFFR/BR3) promotes the survival of mature B-cells and the B-cell response.[1] Isoform 2 seems to inhibit isoform 1 secretion and bioactivity (By similarity).[2] 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 PubMedTALL-1/BAFF/BLyS was recently identified as a member of the tumor necrosis factor (TNF) ligand family. The crystal structure of the functional soluble TALL-1 (sTALL-1) has been determined at 3.0 A. sTALL-1 forms a virus-like assembly with 200 A diameter in the crystals, containing 60 sTALL-1 monomers. The cluster formation is mediated by a "flap" region of the sTALL-1 monomer. The virus-like assembly was also detected in solution using gel filtration and electron microscopy. Deletion of the flap region disrupted the formation of the virus-like assembly. The mutant sTALL-1 still bound its receptor but could not activate NF-kappaB and did not stimulate B lymphocyte proliferation. Finally, we found the virus-like cluster of sTALL-1 exists in physiological condition. We propose that this virus-like assembly of sTALL-1 is the functional unit for TALL-1 in vivo. Crystal structure of sTALL-1 reveals a virus-like assembly of TNF family ligands.,Liu Y, Xu L, Opalka N, Kappler J, Shu HB, Zhang G Cell. 2002 Feb 8;108(3):383-94. PMID:11853672[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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