%A Pompach,Petr %A Viola,Cristina M. %A Radosavljević,Jelena %A Lin,Jingjing %A Jiráček,Jiří %A Brzozowski,Andrzej M. %A Selicharová,Irena %D 2019 %J Frontiers in Endocrinology %C %F %G English %K IGF - I,Imp-L2,Cross-linking,diazirine ring,Mass-spectrometry %Q %R 10.3389/fendo.2019.00695 %W %L %M %P %7 %8 2019-October-09 %9 Original Research %# %! IGF-1 interaction with insect insulin binding protein %* %< %T Cross-Linking/Mass Spectrometry Uncovers Details of Insulin-Like Growth Factor Interaction With Insect Insulin Binding Protein Imp-L2 %U https://www.frontiersin.org/articles/10.3389/fendo.2019.00695 %V 10 %0 JOURNAL ARTICLE %@ 1664-2392 %X 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.