Počet záznamů: 1  

Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2

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    0518634 - MBÚ 2020 RIV CH eng J - Článek v odborném periodiku
    Pompach, Petr - Viola, C. M. - Radosavljević, Jelena - Lin, Jingjing - Jiráček, Jiří - Brzozowski, A. M. - Selicharová, Irena
    Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2.
    Frontiers in Endocrinology. Roč. 10, OCT 9 2019 (2019), č. článku 695. ISSN 1664-2392. E-ISSN 1664-2392
    Grant CEP: GA MŠMT(CZ) EF16_019/0000729
    Institucionální podpora: RVO:61388971 ; RVO:61388963
    Klíčová slova: IGF-1 * diazirine ring * mass spectrometry
    Obor OECD: Biochemistry and molecular biology; Biochemical research methods (UOCHB-X)
    Impakt faktor: 3.644, rok: 2019
    Způsob publikování: Open access
    https://www.frontiersin.org/articles/10.3389/fendo.2019.00695/full

    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.
    Trvalý link: http://hdl.handle.net/11104/0303739

     
     
Počet záznamů: 1  

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