MIRG2010 Study: Molecular Interactions in a Three Component System

r2-2 Protein-protein interactions identified through high-throughput proteomics efforts continue to advance our understanding of the protein interactome; also called the protein-protein interaction network (PPI), or protein interaction network (PIN). In addition to highly specific protein-protein in...

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Bibliographic Details
Published in:	Journal of biomolecular techniques Vol. 21; no. 3 Suppl; p. S15
Main Authors:	Bergqvist, S., Doyle, M.L., Edavettal, S.C., Eisenstein, E., Robinson, M.K., Yadav, S.P., Yeung, A.T., Yamniuk, A.
Format:	Journal Article
Language:	English
Published:	Bethesda, MD Association of Biomolecular Resource Facilities 01-09-2010
Subjects:	Research Group Session Abstracts
Online Access:	Get full text
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Summary:	r2-2 Protein-protein interactions identified through high-throughput proteomics efforts continue to advance our understanding of the protein interactome; also called the protein-protein interaction network (PPI), or protein interaction network (PIN). In addition to highly specific protein-protein interactions, it is becoming increasingly more common for pull-down assays and other proteomics techniques to identify multiple protein ligands which bind to the same target protein. One of the challenges faced by core facilities, is to characterize the assembly of these multi-protein complexes and the competition between multiple protein ligands for a given target. Common questions include … do two protein ligands bind to the same epitope on the target? Overlapping epitopes? Distinct epitopes? If two ligands compete for a given target protein, is the competition a direct blocking mechanism or allosteric competition? Can a ternary complex or multi-protein complex be formed? The MIRG2010 study was designed to assess participants ability to correctly describe the interactions between two protein ligands and their target protein using primarily biosensor technologies such as surface plasmon resonance. Participants were provided with microgram quantities of three proteins (A, B and C) and asked to determine if a ternary A-B-C complex can form, or if ligands B and C bind competitively to protein A. This presentation will summarize the experimental approaches taken to characterize the molecular interactions, the interpretation of the data, and the results obtained using different biosensor instruments.
ISSN:	1524-0215 1943-4731