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NMR tools to detect protein allostery
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DOI：10.1016/j.sbi.2024.102792.png)
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Abstract
En 中文
Allostery is a fundamental mechanism of cellular homeostasis by intra-protein communication between distinct functional sites. It is an internal process of proteins to steer interactions not only with each other but also with other biomolecules such as ligands, lipids, and nucleic acids. In addition, allosteric regulation is particularly important in enzymatic activities. A major challenge in structural and molecular biology today is unraveling allosteric sites in proteins, to elucidate the detailed mechanism of allostery and the development of allosteric drugs. Here we summarize the recently developed tools and approaches which enable the elucidation of regulatory hotspots and correlated motion in biomolecules, focusing primarily on solution -state nuclear magnetic resonance spectroscopy (NMR). These tools open an avenue towards a rational understanding of the mechanism of allostery and provide essential information for the design of allosteric drugs.
Keywords:
3-DIMENSIONAL FOURIER SYNTHESIS
COVARIANCE ANALYSIS
EXACT NOE
ENSEMBLE
RESOLUTION
DYNAMICS
IMPLEMENTATION
ELUCIDATION
MYOGLOBIN
EXCHANGE
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