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Application of surface plasmon resonance for analysis of protein–protein interactions in the G protein‐mediated signal transduction pathway
Author(s) -
Slepak Vladlen Z.
Publication year - 2000
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(200001/02)13:1<20::aid-jmr485>3.0.co;2-n
Subject(s) - heterotrimeric g protein , signal transduction , effector , surface plasmon resonance , microbiology and biotechnology , g protein , g beta gamma complex , protein–protein interaction , biophysics , gtpase activating protein , g protein coupled receptor kinase , receptor , protein kinase a , g protein coupled receptor , chemistry , biology , biochemistry , kinase , nanotechnology , materials science , nanoparticle
Hundreds of extracellular stimuli are received by cells via the pathways consisting of three basic components: cell‐surface receptors, heterotrimeric G proteins, and intracellular effector enzymes or ion channels. A number of additional molecules, including G protein‐coupled receptor kinases (GRKs), phosducin and Ca 2+ ‐binding proteins modulate signal transduction through these cascades. Understanding how these universal pathways work requires a detailed analysis of the interactions between these proteins. The recently emerged technology of surface plasmon resonance (SPR) can study protein–protein interactions by measuring not only the equilibrium binding constants, but also the association and dissociation rates. This article reviews experimental design used by researchers to analyze different components of the G protein pathway by SPR and focuses on the insights this technique provides regarding the kinetics, structure–function aspects and regulation of specific molecular events in the cascade. Copyright © 2000 John Wiley & Sons, Ltd.