dc.contributor.author | Tossavainen, Helena | |
dc.contributor.author | Uğurlu, Hasan | |
dc.contributor.author | Karjalainen, Mikael | |
dc.contributor.author | Hellman, Maarit | |
dc.contributor.author | Antenucci, Lina | |
dc.contributor.author | Fagerlund, Riku | |
dc.contributor.author | Saksela, Kalle | |
dc.contributor.author | Permi, Perttu | |
dc.date.accessioned | 2022-05-02T09:22:14Z | |
dc.date.available | 2022-05-02T09:22:14Z | |
dc.date.issued | 2022 | |
dc.identifier.citation | Tossavainen, H., Uğurlu, H., Karjalainen, M., Hellman, M., Antenucci, L., Fagerlund, R., Saksela, K., & Permi, P. (2022). Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs. <i>Structure</i>, <i>30</i>(6), 828-839.e6. <a href="https://doi.org/10.1016/j.str.2022.03.006" target="_blank">https://doi.org/10.1016/j.str.2022.03.006</a> | |
dc.identifier.other | CONVID_118818289 | |
dc.identifier.uri | https://jyx.jyu.fi/handle/123456789/80830 | |
dc.description.abstract | Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]xØPxxP, the hydrophobic residue Ø being proline or leucine. We have studied the unusual Ø = Ala-specificity of SNX9 SH3 by determining its complex structure with a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The structure revealed the length and composition of the n-Src loop as important factors determining specificity. We also compared the affinities of EEEV nsP3 peptide, its mutants, and cellular ligands to SNX9 SH3. These data suggest that nsP3 has evolved to minimize reduction of conformational entropy upon binding, hence acquiring stronger affinity, enabling takeover of SNX9. The RxAPxxP motif was also found in human T cell leukemia virus-1 (HTLV-1) Gag polyprotein. We found that this motif was required for efficient HTLV-1 infection, and that the specificity of SNX9 SH3 for the RxAPxxP core binding motif was importantly involved in this process. | en |
dc.format.mimetype | application/pdf | |
dc.language.iso | eng | |
dc.publisher | Elsevier | |
dc.relation.ispartofseries | Structure | |
dc.rights | CC BY 4.0 | |
dc.subject.other | EEEV nsP3 | |
dc.subject.other | HTLV-1 Gag | |
dc.subject.other | isothermal titration calorimetry | |
dc.subject.other | SH3 | |
dc.subject.other | SNX9 | |
dc.subject.other | solution NMR spectroscopy | |
dc.title | Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs | |
dc.type | article | |
dc.identifier.urn | URN:NBN:fi:jyu-202205022495 | |
dc.contributor.laitos | Kemian laitos | fi |
dc.contributor.laitos | Bio- ja ympäristötieteiden laitos | fi |
dc.contributor.laitos | Department of Chemistry | en |
dc.contributor.laitos | Department of Biological and Environmental Science | en |
dc.contributor.oppiaine | Fysikaalinen kemia | fi |
dc.contributor.oppiaine | Biologisten vuorovaikutusten huippututkimusyksikkö | fi |
dc.contributor.oppiaine | Nanoscience Center | fi |
dc.contributor.oppiaine | Physical Chemistry | en |
dc.contributor.oppiaine | Centre of Excellence in Biological Interactions Research | en |
dc.contributor.oppiaine | Nanoscience Center | en |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | |
dc.type.coar | http://purl.org/coar/resource_type/c_2df8fbb1 | |
dc.description.reviewstatus | peerReviewed | |
dc.format.pagerange | 828-839.e6 | |
dc.relation.issn | 0969-2126 | |
dc.relation.numberinseries | 6 | |
dc.relation.volume | 30 | |
dc.type.version | publishedVersion | |
dc.rights.copyright | © 2022 The Author(s). Published by Elsevier Ltd. | |
dc.rights.accesslevel | openAccess | fi |
dc.relation.grantnumber | 323435 | |
dc.subject.yso | proteiinit | |
dc.subject.yso | soluviestintä | |
dc.subject.yso | virukset | |
dc.subject.yso | alfavirukset | |
dc.subject.yso | retrovirukset | |
dc.format.content | fulltext | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p4332 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p28740 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p1123 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p22268 | |
jyx.subject.uri | http://www.yso.fi/onto/yso/p16805 | |
dc.rights.url | https://creativecommons.org/licenses/by/4.0/ | |
dc.relation.doi | 10.1016/j.str.2022.03.006 | |
dc.relation.funder | Research Council of Finland | en |
dc.relation.funder | Suomen Akatemia | fi |
jyx.fundingprogram | Academy Project, AoF | en |
jyx.fundingprogram | Akatemiahanke, SA | fi |
jyx.fundinginformation | This work is supported by the Jane and Aatos Erkko Foundation and grants from the Academy of Finland (grant 323435 to P.P.) and Helsinki University Central Hospital Research Council (grant TYH2020239 to K.S.). H.U. has been supported by the Turkish Ministry of National Education. | |
dc.type.okm | A1 | |