4zg0

From Proteopedia

(Difference between revisions)

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

Personal tools

Navigation

Search

Toolbox