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

Overview

Journal Front Endocrinol (Lausanne)

Specialty Endocrinology

Date 2019 Oct 26

PMID 31649623

Citations 1

Authors

Petr Pompach

Cristina M Viola

Jelena Radosavljevic

Jingjing Lin

Jiri Jiracek

Andrzej M Brzozowski

Irena Selicharova

Affiliations

Soon will be listed here.

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): 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 -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.

Citing Articles

The Continuing Evolution of Insulin-like Growth Factor Signaling.

Rosenzweig S F1000Res. 2020; 9.

PMID: 32226608 PMC: 7096212. DOI: 10.12688/f1000research.22198.1.

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