This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
4zg0
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
== 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. | [[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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:26100207</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4zg0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 08:18, 1 June 2016
Crystal structure of Mouse Syndesmos protein
| |||||||||||
