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| | ==Solution structure of the link module of human tsg-6 in presence of a chondroitin 4-sulfate hexasaccharide== | | ==Solution structure of the link module of human tsg-6 in presence of a chondroitin 4-sulfate hexasaccharide== |
| - | <StructureSection load='2n40' size='340' side='right'caption='[[2n40]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2n40' size='340' side='right'caption='[[2n40]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2n40]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N40 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N40 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2n40]] 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=2N40 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N40 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TNFAIP6, TSG6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2n40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n40 OCA], [https://pdbe.org/2n40 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n40 RCSB], [https://www.ebi.ac.uk/pdbsum/2n40 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n40 ProSAT]</span></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=2n40 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n40 OCA], [http://pdbe.org/2n40 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n40 RCSB], [http://www.ebi.ac.uk/pdbsum/2n40 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n40 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TSG6_HUMAN TSG6_HUMAN]] Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis. | + | [https://www.uniprot.org/uniprot/TSG6_HUMAN TSG6_HUMAN] Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis. |
| | <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: Park, Y]] | + | [[Category: Park Y]] |
| - | [[Category: Prestegard, J H]] | + | [[Category: Prestegard JH]] |
| - | [[Category: Cell adhesion]]
| + | |
| - | [[Category: Chondroitin sulfate]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Link module]]
| + | |
| - | [[Category: Tsg-6]]
| + | |
| Structural highlights
Function
TSG6_HUMAN Possibly involved in cell-cell and cell-matrix interactions during inflammation and tumorigenesis.
Publication Abstract from PubMed
Tumor necrosis factor-stimulated gene-6 (TSG-6) is a hyaluronan (HA)-binding protein that is essential for stabilizing and remodeling the extracellular matrix (ECM) during ovulation and inflammatory disease processes such as arthritis. The Link module, one of the domains of TSG-6, is responsible for binding hyaluronan and other glycosaminoglycans found in the ECM. In this study, we used a well-defined chondroitin sulfate (CS) hexasaccharide (DeltaC444S) to determine the structure of the Link module, in solution, in its chondroitin sulfate-bound state. A variety of nuclear magnetic resonance techniques were employed, including chemical shift perturbation, residual dipolar couplings (RDCs), nuclear Overhauser effects, spin relaxation measurements, and paramagnetic relaxation enhancements from a spin-labeled analogue of DeltaC444S. The binding site for DeltaC444S on the Link module overlapped with that of HA. Surprisingly, DeltaC444S binding induced dimerization of the Link module (as confirmed by analytical ultracentrifugation), and a second weak binding site that partially overlapped with a previously identified heparin site was detected. A dimer model was generated using chemical shift perturbations and RDCs as restraints in the docking program HADDOCK. We postulate that the molecular cross-linking enhanced by the multiple binding modes of the Link module might be critical for remodeling the ECM during inflammation/ovulation and might contribute to other functions of TSG-6.
Nuclear Magnetic Resonance Insight into the Multiple Glycosaminoglycan Binding Modes of the Link Module from Human TSG-6.,Park Y, Jowitt TA, Day AJ, Prestegard JH Biochemistry. 2016 Jan 6. PMID:26685054[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Park Y, Jowitt TA, Day AJ, Prestegard JH. Nuclear Magnetic Resonance Insight into the Multiple Glycosaminoglycan Binding Modes of the Link Module from Human TSG-6. Biochemistry. 2016 Jan 6. PMID:26685054 doi:http://dx.doi.org/10.1021/acs.biochem.5b01148
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