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Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2
dc.creator | Pompach, Petr | |
dc.creator | Viola, Cristina M. | |
dc.creator | Radosavljević, Jelena | |
dc.creator | Lin, Jingjing | |
dc.creator | Jiráček, Jirˇí | |
dc.creator | Brzozowski, Andrzej M. | |
dc.creator | Selicharová, Irena | |
dc.date.accessioned | 2019-12-02T10:58:33Z | |
dc.date.available | 2019-12-02T10:58:33Z | |
dc.date.issued | 2019 | |
dc.identifier.issn | 1664-2392 | |
dc.identifier.uri | https://cherry.chem.bg.ac.rs/handle/123456789/3719 | |
dc.description.abstract | Structural details of changes accompanying interaction between insulin-related hormones and their binding partners are often enigmatic. Here, cross-linking/mass spectrometry could complement structural techniques and reveal details of these protein-protein interfaces. We used such approach to clarify missing structural description of the interface in human insulin-like growth factor (IGF-1): Drosophila melanogaster imaginal morphogenesis protein-late 2 protein (Imp-L2) complex which we studied previously by X-ray crystallography. We crosslinked these proteins by heterobifunctional cross-linker sulfosuccinimidyl 4,4′-azidopentanoate (Sulfo-SDA) for the subsequent mass spectrometry (MS) analysis. The MS analysis revealed IGF-1:Imp-L2 interactions which were not resolved in the crystal structure of this assembly, and they converged with X-ray results, indicating the importance of the IGF-1 N-terminus interaction with the C-terminal (185–242) part of the Imp-L2 for stability of this complex. Here, we also showed the advantage and reliability of MS approach in solving details of protein-protein interactions that are too flexible for solid state structural methods. | |
dc.publisher | Frontiers Media S.A. | |
dc.relation | Medical Research Council Grants MR/K000179/1 and MR/R009066/1 | |
dc.relation | Chemical biology for drugging undruggable targets (ChemBioDrug) (No. CZ.02.1.01/0.0/0.0/16_019/0000729) | |
dc.relation | Czech Infrastructure for Integrative Structural Biology (LM2015043 CIISB for CMS BIOCEV funded by MEYS CR) | |
dc.rights | openAccess | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.source | Frontiers in Endocrinology | |
dc.subject | cross-linking | |
dc.subject | diazirine ring | |
dc.subject | IGF-1 | |
dc.subject | Imp-L2 | |
dc.subject | mass spectrometry | |
dc.title | Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2 | |
dc.type | article | |
dc.rights.license | BY | |
dcterms.abstract | Виола, Цристина М.; Лин, Јингјинг; Јирáчек, Јирˇí; Селицхаровá, Ирена; Помпацх, Петр; Брзозоwски, Aндрзеј М.; Радосављевић, Јелена; | |
dc.citation.volume | 10 | |
dc.identifier.wos | 000497451900001 | |
dc.identifier.doi | 10.3389/fendo.2019.00695 | |
dc.citation.rank | M22~ | |
dc.description.other | Supplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/3720] | |
dc.type.version | publishedVersion | |
dc.identifier.scopus | 2-s2.0-85074154541 | |
dc.identifier.fulltext | https://cherry.chem.bg.ac.rs/bitstream/id/16277/Cross-Linking_Mass_pub_2019.pdf |