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1osg

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(New page: 200px<br /> <applet load="1osg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1osg, resolution 3.00&Aring;" /> '''Complex between BAF...)
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[[Image:1osg.gif|left|200px]]<br />
 
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<applet load="1osg" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1osg, resolution 3.00&Aring;" />
 
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'''Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold'''<br />
 
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==Overview==
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==Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold==
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BAFF/BLyS, a member of the tumor necrosis family (TNF) superfamily of, ligands, is a crucial survival factor for B cells. BAFF binds three, receptors, TACI, BCMA, and BR3, with signaling through BR3 being essential, for promoting B cell function. Typical TNF receptor (TNFR) family members, bind their cognate ligands through interactions with two cysteine-rich, domains (CRDs). However, the extracellular domain (ECD) of BR3 consists of, only a partial CRD, with cysteine spacing distinct from other modules, described previously. Herein, we report the solution structure of the BR3, ECD. A core region of only 19 residues adopts a stable structure in, solution. The BR3 fold is analogous to the first half of a canonical TNFR, CRD but is stabilized by an additional noncanonical disulfide bond., BAFF-binding determinants were identified by shotgun alanine-scanning, mutagenesis of the BR3 ECD expressed on phage. Several of the key, BAFF-binding residues are presented from a beta-turn that we have shown, previously to be sufficient for ligand binding when transferred to a, structured beta-hairpin scaffold [Kayagaki, N., Yan, M., Seshasayee, D., Wang, H., Lee, W., French, D. M., Grewal, I. S., Cochran, A. G., Gordon, N. C., Yin, J., Starovasnik, M. A, and Dixit, V. M. (2002) Immunity 10, 515-524]. Outside of the turn, mutagenesis identifies additional, hydrophobic contacts that enhance the BAFF-BR3 interaction. The crystal, structure of the minimal hairpin peptide, bhpBR3, in complex with BAFF, reveals intimate packing of the six-residue BR3 turn into a cavity on the, ligand surface. Thus, BR3 binds BAFF through a highly focused interaction, site, unprecedented in the TNFR family.
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<StructureSection load='1osg' size='340' side='right'caption='[[1osg]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1osg]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OSG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1osg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1osg OCA], [https://pdbe.org/1osg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1osg RCSB], [https://www.ebi.ac.uk/pdbsum/1osg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1osg ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/TN13B_HUMAN 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.<ref>PMID:10973284</ref> Isoform 2 seems to inhibit isoform 1 secretion and bioactivity (By similarity).<ref>PMID:10973284</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/os/1osg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1osg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BAFF/BLyS, a member of the tumor necrosis family (TNF) superfamily of ligands, is a crucial survival factor for B cells. BAFF binds three receptors, TACI, BCMA, and BR3, with signaling through BR3 being essential for promoting B cell function. Typical TNF receptor (TNFR) family members bind their cognate ligands through interactions with two cysteine-rich domains (CRDs). However, the extracellular domain (ECD) of BR3 consists of only a partial CRD, with cysteine spacing distinct from other modules described previously. Herein, we report the solution structure of the BR3 ECD. A core region of only 19 residues adopts a stable structure in solution. The BR3 fold is analogous to the first half of a canonical TNFR CRD but is stabilized by an additional noncanonical disulfide bond. BAFF-binding determinants were identified by shotgun alanine-scanning mutagenesis of the BR3 ECD expressed on phage. Several of the key BAFF-binding residues are presented from a beta-turn that we have shown previously to be sufficient for ligand binding when transferred to a structured beta-hairpin scaffold [Kayagaki, N., Yan, M., Seshasayee, D., Wang, H., Lee, W., French, D. M., Grewal, I. S., Cochran, A. G., Gordon, N. C., Yin, J., Starovasnik, M. A, and Dixit, V. M. (2002) Immunity 10, 515-524]. Outside of the turn, mutagenesis identifies additional hydrophobic contacts that enhance the BAFF-BR3 interaction. The crystal structure of the minimal hairpin peptide, bhpBR3, in complex with BAFF reveals intimate packing of the six-residue BR3 turn into a cavity on the ligand surface. Thus, BR3 binds BAFF through a highly focused interaction site, unprecedented in the TNFR family.
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==About this Structure==
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BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site.,Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA Biochemistry. 2003 May 27;42(20):5977-83. PMID:12755599<ref>PMID:12755599</ref>
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1OSG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OSG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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BAFF/BLyS receptor 3 comprises a minimal TNF receptor-like module that encodes a highly focused ligand-binding site., Gordon NC, Pan B, Hymowitz SG, Yin J, Kelley RF, Cochran AG, Yan M, Dixit VM, Fairbrother WJ, Starovasnik MA, Biochemistry. 2003 May 27;42(20):5977-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12755599 12755599]
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</div>
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[[Category: Homo sapiens]]
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<div class="pdbe-citations 1osg" style="background-color:#fffaf0;"></div>
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[[Category: Single protein]]
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[[Category: Cochran, A.G.]]
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[[Category: Dixit, V.M.]]
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[[Category: Fairbrother, W.J.]]
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[[Category: Gordon, N.C.]]
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[[Category: Hymowitz, S.G.]]
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[[Category: Kelley, R.F.]]
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[[Category: Pan, B.]]
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[[Category: Starovasnik, M.A.]]
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[[Category: Yan, M.]]
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[[Category: Yin, J.P.]]
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[[Category: MG]]
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[[Category: beta hairpin]]
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[[Category: jelly-roll]]
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[[Category: protein-peptide complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:36:12 2007''
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==See Also==
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*[[Tumor necrosis factor receptor 3D structures|Tumor necrosis factor receptor 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Cochran AG]]
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[[Category: Dixit VM]]
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[[Category: Fairbrother WJ]]
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[[Category: Gordon NC]]
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[[Category: Hymowitz SG]]
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[[Category: Kelley RF]]
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[[Category: Pan B]]
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[[Category: Starovasnik MA]]
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[[Category: Yan M]]
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[[Category: Yin JP]]

Current revision

Complex between BAFF and a BR3 derived peptide presented in a beta-hairpin scaffold

PDB ID 1osg

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