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| | ==Crystal structure of Mouse Syndesmos protein== | | ==Crystal structure of Mouse Syndesmos protein== |
| - | <StructureSection load='4zg0' size='340' side='right' caption='[[4zg0]], [[Resolution|resolution]] 2.01Å' scene=''> | + | <StructureSection load='4zg0' size='340' side='right'caption='[[4zg0]], [[Resolution|resolution]] 2.01Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zg0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZG0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZG0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zg0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZG0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Nudt16l1, Sdos ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.006Å</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=4zg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zg0 OCA], [http://pdbe.org/4zg0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zg0 RCSB], [http://www.ebi.ac.uk/pdbsum/4zg0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zg0 ProSAT]</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=4zg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zg0 OCA], [https://pdbe.org/4zg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zg0 RCSB], [https://www.ebi.ac.uk/pdbsum/4zg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zg0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SDOS_MOUSE SDOS_MOUSE]] Does not play a role in U8 snoRNA decapping activity. Binds U8 snoRNA (By similarity). Probable adapter protein, which may link syndecan-4 (SDC4) and paxilin (TGFB1I1 and PXN) receptors. | + | [https://www.uniprot.org/uniprot/TIRR_MOUSE TIRR_MOUSE] Key regulator of TP53BP1 required to stabilize TP53BP1 and regulate its recruitment to chromatin. In absence of DNA damage, interacts with the tandem Tudor-like domain of TP53BP1, masking the region that binds histone H4 dimethylated at 'Lys-20' (H4K20me2), thereby preventing TP53BP1 recruitment to chromatin and maintaining TP53BP1 localization to the nucleus. Following DNA damage, ATM-induced phosphorylation of TP53BP1 and subsequent recruitment of RIF1 leads to dissociate NUDT16L1/TIRR from TP53BP1, unmasking the tandem Tudor-like domain and allowing recruitment of TP53BP1 to DNA double strand breaks (DSBs). Binds U8 snoRNA.[UniProtKB:Q9BRJ7] |
| | <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: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Cho, H]] | + | [[Category: Mus musculus]] |
| - | [[Category: Kim, H]] | + | [[Category: Cho H]] |
| - | [[Category: Lee, I]] | + | [[Category: Kim H]] |
| - | [[Category: Lee, W]] | + | [[Category: Lee I]] |
| - | [[Category: Yoo, J]] | + | [[Category: Lee W]] |
| - | [[Category: Cytoplasmic protein]]
| + | [[Category: Yoo J]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nudix hydrolase]]
| + | |
| - | [[Category: Syndecan-4 cytoplasmic domain interactor]]
| + | |
| Structural highlights
Function
TIRR_MOUSE Key regulator of TP53BP1 required to stabilize TP53BP1 and regulate its recruitment to chromatin. In absence of DNA damage, interacts with the tandem Tudor-like domain of TP53BP1, masking the region that binds histone H4 dimethylated at 'Lys-20' (H4K20me2), thereby preventing TP53BP1 recruitment to chromatin and maintaining TP53BP1 localization to the nucleus. Following DNA damage, ATM-induced phosphorylation of TP53BP1 and subsequent recruitment of RIF1 leads to dissociate NUDT16L1/TIRR from TP53BP1, unmasking the tandem Tudor-like domain and allowing recruitment of TP53BP1 to DNA double strand breaks (DSBs). Binds U8 snoRNA.[UniProtKB:Q9BRJ7]
Publication Abstract from PubMed
Syndesmos, nucleoside diphosphate linked moiety X (nudix)-type motif 16-like 1 (Nudt16l1), is evolutionarily divergent from the Nudt16 family. Syndesmos, which is co-localized with syndecan-4 cytoplasmic domain (Syn4(cyto)) in focal contacts, interacts with various cell adhesion adaptor proteins to control cell signaling. We determined the X-ray crystal structure of syndesmos; it is composed of seven alpha-helices and seven beta-strands. Although syndesmos has a molecular topology similar to that of nudix hydrolase proteins, the structure of the nudix motif differs from that of X29. The dimeric interface of syndesmos is composed of alpha-helix 4, 7 and beta-strand 2, 7, which primarily form hydrophobic interactions. The binding interaction between syndesmos and syn4(cyto) was characterized as a low-affinity interaction (Kd = 62 muM) by surface plasmon resonance (SPR) and nuclear magnetic resonance (NMR). The NMR resonances of Lys (177, 178, 179), Gly182, and Ser183 in the C1 region and Lys193 and Lys194 in the V region of syndecan-4 are perturbed upon syndesmos binding. Our results provide structural insight into the molecular function of syndesmos in the regulation of cell signaling via binding to syndecan-4.
Crystal structure of syndesmos and its interaction with Syndecan-4 proteoglycan.,Kim H, Yoo J, Lee I, Kang YJ, Cho HS, Lee W Biochem Biophys Res Commun. 2015 Aug 7;463(4):762-7. doi:, 10.1016/j.bbrc.2015.06.010. Epub 2015 Jun 19. PMID:26100207[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim H, Yoo J, Lee I, Kang YJ, Cho HS, Lee W. Crystal structure of syndesmos and its interaction with Syndecan-4 proteoglycan. Biochem Biophys Res Commun. 2015 Aug 7;463(4):762-7. doi:, 10.1016/j.bbrc.2015.06.010. Epub 2015 Jun 19. PMID:26100207 doi:http://dx.doi.org/10.1016/j.bbrc.2015.06.010
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