2qe3: Difference between revisions

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[[Image:2qe3.png|left|200px]]


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==Crystal structure of human tl1a extracellular domain==
The line below this paragraph, containing "STRUCTURE_2qe3", creates the "Structure Box" on the page.
<StructureSection load='2qe3' size='340' side='right'caption='[[2qe3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2qe3]] is a 1 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=2QE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QE3 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=CL:CHLORIDE+ION'>CL</scene></td></tr>
{{STRUCTURE_2qe3|  PDB=2qe3  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qe3 OCA], [https://pdbe.org/2qe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qe3 RCSB], [https://www.ebi.ac.uk/pdbsum/2qe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qe3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TNF15_HUMAN TNF15_HUMAN] Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis.<ref>PMID:9872942</ref> <ref>PMID:11923219</ref> <ref>PMID:11911831</ref> <ref>PMID:10597252</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qe/2qe3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=2qe3 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
TNF-like 1A (TL1A) is a newly described member of the TNF superfamily that is directly implicated in the pathogenesis of autoimmune diseases, including inflammatory bowel disease, atherosclerosis, and rheumatoid arthritis. We report the crystal structure of the human TL1A extracellular domain at a resolution of 2.5 A, which reveals a jelly-roll fold typical of the TNF superfamily. This structural information, in combination with complementary mutagenesis and biochemical characterization, provides insights into the binding interface and the specificity of the interactions between TL1A and the DcR3 and DR3 receptors. These studies suggest that the mode of interaction between TL1A and DcR3 differs from other characterized TNF ligand/receptor complexes. In addition, we have generated functional TL1A mutants with altered disulfide bonding capability that exhibit enhanced solution properties, which will facilitate the production of materials for future cell-based and whole animal studies. In summary, these studies provide insights into the structure and function of TL1A and provide the basis for the rational manipulation of its interactions with cognate receptors.


===Crystal structure of human tl1a extracellular domain===
Biochemical and structural characterization of the human TL1A ectodomain.,Zhan C, Yan Q, Patskovsky Y, Li Z, Toro R, Meyer A, Cheng H, Brenowitz M, Nathenson SG, Almo SC Biochemistry. 2009 Aug 18;48(32):7636-45. PMID:19522538<ref>PMID:19522538</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2qe3" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_19522538}}, adds the Publication Abstract to the page
*[[Tumor necrosis factor ligand superfamily 3D structures|Tumor necrosis factor ligand superfamily 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 19522538 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_19522538}}
__TOC__
 
</StructureSection>
==About this Structure==
2QE3 is a 1 chain structure of sequence 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=2QE3 OCA].
 
==Reference==
<ref group="xtra">PMID:19522538</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Almo, S C.]]
[[Category: Large Structures]]
[[Category: Bonanno, J.]]
[[Category: Almo SC]]
[[Category: Nathenson, S G.]]
[[Category: Bonanno J]]
[[Category: Patskovsky, Y.]]
[[Category: Nathenson SG]]
[[Category: Shi, W.]]
[[Category: Patskovsky Y]]
[[Category: Toro, R.]]
[[Category: Shi W]]
[[Category: Yan, Q.]]
[[Category: Toro R]]
[[Category: Zhan, C.]]
[[Category: Yan Q]]
[[Category: Cytokine]]
[[Category: Zhan C]]
[[Category: Tl1a]]
[[Category: Tnfsf]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 30 08:43:46 2009''

Latest revision as of 14:29, 30 August 2023

Crystal structure of human tl1a extracellular domainCrystal structure of human tl1a extracellular domain

Structural highlights

2qe3 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

TNF15_HUMAN Receptor for TNFRSF25 and TNFRSF6B. Mediates activation of NF-kappa-B. Inhibits vascular endothelial growth and angiogenesis (in vitro). Promotes activation of caspases and apoptosis.[1] [2] [3] [4]

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

TNF-like 1A (TL1A) is a newly described member of the TNF superfamily that is directly implicated in the pathogenesis of autoimmune diseases, including inflammatory bowel disease, atherosclerosis, and rheumatoid arthritis. We report the crystal structure of the human TL1A extracellular domain at a resolution of 2.5 A, which reveals a jelly-roll fold typical of the TNF superfamily. This structural information, in combination with complementary mutagenesis and biochemical characterization, provides insights into the binding interface and the specificity of the interactions between TL1A and the DcR3 and DR3 receptors. These studies suggest that the mode of interaction between TL1A and DcR3 differs from other characterized TNF ligand/receptor complexes. In addition, we have generated functional TL1A mutants with altered disulfide bonding capability that exhibit enhanced solution properties, which will facilitate the production of materials for future cell-based and whole animal studies. In summary, these studies provide insights into the structure and function of TL1A and provide the basis for the rational manipulation of its interactions with cognate receptors.

Biochemical and structural characterization of the human TL1A ectodomain.,Zhan C, Yan Q, Patskovsky Y, Li Z, Toro R, Meyer A, Cheng H, Brenowitz M, Nathenson SG, Almo SC Biochemistry. 2009 Aug 18;48(32):7636-45. PMID:19522538[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Zhai Y, Ni J, Jiang GW, Lu J, Xing L, Lincoln C, Carter KC, Janat F, Kozak D, Xu S, Rojas L, Aggarwal BB, Ruben S, Li LY, Gentz R, Yu GL. VEGI, a novel cytokine of the tumor necrosis factor family, is an angiogenesis inhibitor that suppresses the growth of colon carcinomas in vivo. FASEB J. 1999 Jan;13(1):181-9. PMID:9872942
  2. ↑ Chew LJ, Pan H, Yu J, Tian S, Huang WQ, Zhang JY, Pang S, Li LY. A novel secreted splice variant of vascular endothelial cell growth inhibitor. FASEB J. 2002 May;16(7):742-4. Epub 2002 Mar 26. PMID:11923219 doi:10.1096/fj.01-0757fje
  3. ↑ Migone TS, Zhang J, Luo X, Zhuang L, Chen C, Hu B, Hong JS, Perry JW, Chen SF, Zhou JX, Cho YH, Ullrich S, Kanakaraj P, Carrell J, Boyd E, Olsen HS, Hu G, Pukac L, Liu D, Ni J, Kim S, Gentz R, Feng P, Moore PA, Ruben SM, Wei P. TL1A is a TNF-like ligand for DR3 and TR6/DcR3 and functions as a T cell costimulator. Immunity. 2002 Mar;16(3):479-92. PMID:11911831
  4. ↑ Haridas V, Shrivastava A, Su J, Yu GL, Ni J, Liu D, Chen SF, Ni Y, Ruben SM, Gentz R, Aggarwal BB. VEGI, a new member of the TNF family activates nuclear factor-kappa B and c-Jun N-terminal kinase and modulates cell growth. Oncogene. 1999 Nov 11;18(47):6496-504. PMID:10597252 doi:10.1038/sj.onc.1203059
  5. ↑ Zhan C, Yan Q, Patskovsky Y, Li Z, Toro R, Meyer A, Cheng H, Brenowitz M, Nathenson SG, Almo SC. Biochemical and structural characterization of the human TL1A ectodomain. Biochemistry. 2009 Aug 18;48(32):7636-45. PMID:19522538 doi:10.1021/bi900031w

2qe3, resolution 2.50Å

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