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| | <StructureSection load='1n99' size='340' side='right'caption='[[1n99]], [[Resolution|resolution]] 1.94Å' scene=''> | | <StructureSection load='1n99' size='340' side='right'caption='[[1n99]], [[Resolution|resolution]] 1.94Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1n99]] is a 2 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=1N99 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1N99 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1n99]] is a 2 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=1N99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N99 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SDCBP OR MDA9 OR SYCL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1n99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n99 OCA], [https://pdbe.org/1n99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n99 RCSB], [https://www.ebi.ac.uk/pdbsum/1n99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n99 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1n99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n99 OCA], [http://pdbe.org/1n99 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n99 RCSB], [http://www.ebi.ac.uk/pdbsum/1n99 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n99 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SDCB1_HUMAN SDCB1_HUMAN]] Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.<ref>PMID:10230395</ref> <ref>PMID:11179419</ref> <ref>PMID:11498591</ref> | + | [https://www.uniprot.org/uniprot/SDCB1_HUMAN SDCB1_HUMAN] Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.<ref>PMID:10230395</ref> <ref>PMID:11179419</ref> <ref>PMID:11498591</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1n99" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1n99" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[3D structures of syntenin|3D structures of syntenin]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cooper, D R]] | + | [[Category: Cooper DR]] |
| - | [[Category: Dauter, Z]] | + | [[Category: Dauter Z]] |
| - | [[Category: Derewenda, U]] | + | [[Category: Derewenda U]] |
| - | [[Category: Derewenda, Z S]] | + | [[Category: Derewenda ZS]] |
| - | [[Category: Devedjiev, Y]] | + | [[Category: Devedjiev Y]] |
| - | [[Category: Jelen, F]] | + | [[Category: Jelen F]] |
| - | [[Category: Kang, B S]] | + | [[Category: Kang BS]] |
| - | [[Category: Otlewski, J]] | + | [[Category: Otlewski J]] |
| - | [[Category: Pdz domain]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
SDCB1_HUMAN Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.[1] [2] [3]
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
Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin.
PDZ tandem of human syntenin: crystal structure and functional properties.,Kang BS, Cooper DR, Jelen F, Devedjiev Y, Derewenda U, Dauter Z, Otlewski J, Derewenda ZS Structure. 2003 Apr;11(4):459-68. PMID:12679023[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fernandez-Larrea J, Merlos-Suarez A, Urena JM, Baselga J, Arribas J. A role for a PDZ protein in the early secretory pathway for the targeting of proTGF-alpha to the cell surface. Mol Cell. 1999 Apr;3(4):423-33. PMID:10230395
- ↑ Zimmermann P, Tomatis D, Rosas M, Grootjans J, Leenaerts I, Degeest G, Reekmans G, Coomans C, David G. Characterization of syntenin, a syndecan-binding PDZ protein, as a component of cell adhesion sites and microfilaments. Mol Biol Cell. 2001 Feb;12(2):339-50. PMID:11179419
- ↑ Geijsen N, Uings IJ, Pals C, Armstrong J, McKinnon M, Raaijmakers JA, Lammers JW, Koenderman L, Coffer PJ. Cytokine-specific transcriptional regulation through an IL-5Ralpha interacting protein. Science. 2001 Aug 10;293(5532):1136-8. PMID:11498591 doi:http://dx.doi.org/10.1126/science.1059157
- ↑ Kang BS, Cooper DR, Jelen F, Devedjiev Y, Derewenda U, Dauter Z, Otlewski J, Derewenda ZS. PDZ tandem of human syntenin: crystal structure and functional properties. Structure. 2003 Apr;11(4):459-68. PMID:12679023
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