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4zg0

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Revision as of 07:26, 18 May 2023

Crystal structure of Mouse Syndesmos protein

Structural highlights

4zg0 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4zg0"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Mouse Syndesmos protein==
-<StructureSection load='4zg0' size='340' side='right' caption='[[4zg0]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
+<StructureSection load='4zg0' size='340' side='right'caption='[[4zg0]], [[Resolution|resolution]] 2.01&Aring;' scene=''>
 == 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='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>
-<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>
 </table>
 == 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;">
 == Publication Abstract from PubMed ==
@@ Line 22: / Line 21: @@
 __TOC__
 </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]]

4zg0

From Proteopedia

Revision as of 07:26, 18 May 2023

Crystal structure of Mouse Syndesmos protein

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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