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Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2
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SYSNO ASEP 0518634 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2 Tvůrce(i) Pompach, Petr (MBU-M) RID, ORCID
Viola, C. M. (GB)
Radosavljević, Jelena (UOCHB-X) ORCID, RID
Lin, Jingjing (UOCHB-X)
Jiráček, Jiří (UOCHB-X) RID, ORCID
Brzozowski, A. M. (GB)
Selicharová, Irena (UOCHB-X) RID, ORCIDČíslo článku 695 Zdroj.dok. Frontiers in Endocrinology. - : Frontiers Media - ISSN 1664-2392
Roč. 10, OCT 9 2019 (2019)Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova IGF-1 ; diazirine ring ; mass spectrometry Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology Vědní obor RIV – spolupráce Ústav organické chemie a biochemie - Biochemie CEP EF16_019/0000729 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 ; UOCHB-X - RVO:61388963 UT WOS 000497451900001 EID SCOPUS 85074154541 DOI 10.3389/fendo.2019.00695 Anotace 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 crosslinker 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. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2020 Elektronická adresa https://www.frontiersin.org/articles/10.3389/fendo.2019.00695/full
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