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| | ==Solution structure of Fn14 CRD domain== | | ==Solution structure of Fn14 CRD domain== |
| - | <StructureSection load='2rpj' size='340' side='right'caption='[[2rpj]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2rpj' size='340' side='right'caption='[[2rpj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RPJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rpj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RPJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RPJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2eqp|2eqp]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNFRSF12A, FN14 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2rpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpj OCA], [https://pdbe.org/2rpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rpj RCSB], [https://www.ebi.ac.uk/pdbsum/2rpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rpj ProSAT], [https://www.topsan.org/Proteins/RSGI/2rpj TOPSAN]</span></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=2rpj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rpj OCA], [https://pdbe.org/2rpj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rpj RCSB], [https://www.ebi.ac.uk/pdbsum/2rpj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rpj ProSAT], [https://www.topsan.org/Proteins/RSGI/2rpj TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TNR12_HUMAN TNR12_HUMAN]] Receptor for TNFSF12/TWEAK. Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins.<ref>PMID:11728344</ref>
| + | [https://www.uniprot.org/uniprot/TNR12_HUMAN TNR12_HUMAN] Receptor for TNFSF12/TWEAK. Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins.<ref>PMID:11728344</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dang, W]] | + | [[Category: Dang W]] |
| - | [[Category: He, F]] | + | [[Category: He F]] |
| - | [[Category: Inoue, M]] | + | [[Category: Inoue M]] |
| - | [[Category: Kigawa, T]] | + | [[Category: Kigawa T]] |
| - | [[Category: Muto, Y]] | + | [[Category: Muto Y]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Shirouzu M]] |
| - | [[Category: Shirouzu, M]] | + | [[Category: Terada T]] |
| - | [[Category: Terada, T]] | + | [[Category: Yokoyama S]] |
| - | [[Category: Yokoyama, S]] | + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Angiogenesis]]
| + | |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Developmental protein]]
| + | |
| - | [[Category: Differentiation]]
| + | |
| - | [[Category: Fn14]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: National project on protein structural and functional analyse]]
| + | |
| - | [[Category: Nppsfa]]
| + | |
| - | [[Category: Receptor]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| Structural highlights
Function
TNR12_HUMAN Receptor for TNFSF12/TWEAK. Weak inducer of apoptosis in some cell types. Promotes angiogenesis and the proliferation of endothelial cells. May modulate cellular adhesion to matrix proteins.[1]
Publication Abstract from PubMed
Fn14 is the smallest member of the tumor necrosis factor (TNF) receptor superfamily, and specifically binds to its ligand, TWEAK (TNF-like weak inducer of apoptosis), which is a member of the TNF superfamily. The receptor-ligand recognition between Fn14 and TWEAK induces a variety of cellular processes for tissue remodeling and is also involved in the pathogenesis of some human diseases, such as cancer, chronic autoimmune diseases, and acute ischaemic stroke. The extracellular ligand-binding region of Fn14 is composed of 53 amino acid residues and forms a single, cysteine-rich domain (CRD). In this study, we determined the solution structure of the Fn14 CRD (Glu28-Ala70) by heteronuclear NMR, with a (13)C-/(15)N-labeled sample. The tertiary structure of the CRD comprises a beta-sheet with two strands, followed by a 3(10) helix and a C-terminal alpha-helix, and is stabilized by three disulfide bonds connecting Cys36-Cys49, Cys52-Cys67, and Cys55-Cys64. Comparison of the disulfide bond connectivities and the tertiary structures with those of other CRDs revealed that the Fn14 CRD is similar to the fourth CRD of TNF receptor 1 (A1-C2 module type), but not to the CRD of B-cell maturation antigen and the second CRD of transmembrane activator and CAML (calcium modulator and cyclophilin ligand) interactor (A1-D2 module type). This is the first structural report about the A1-C2 type CRD that could bind to the known target.
Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily.,He F, Dang W, Saito K, Watanabe S, Kobayashi N, Guntert P, Kigawa T, Tanaka A, Muto Y, Yokoyama S Protein Sci. 2009 Mar;18(3):650-6. PMID:19241374[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wiley SR, Cassiano L, Lofton T, Davis-Smith T, Winkles JA, Lindner V, Liu H, Daniel TO, Smith CA, Fanslow WC. A novel TNF receptor family member binds TWEAK and is implicated in angiogenesis. Immunity. 2001 Nov;15(5):837-46. PMID:11728344
- ↑ He F, Dang W, Saito K, Watanabe S, Kobayashi N, Guntert P, Kigawa T, Tanaka A, Muto Y, Yokoyama S. Solution structure of the cysteine-rich domain in Fn14, a member of the tumor necrosis factor receptor superfamily. Protein Sci. 2009 Mar;18(3):650-6. PMID:19241374 doi:10.1002/pro.49
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