The ensemble nature of allostery
By H. Motlagh, James O. Wrabl, Jing Li, V. Hilser. Nature, 2014
1,152 citations recorded by the source corpus.
Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems.
Subfields: Molecular Biology, Spectroscopy
View Paper: https://www.semanticscholar.org/paper/a62b46f4fe8ad073bc1f0b7e07831484be513f06
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In Molecular Biology
- Lauren L. Porter
- M. Grimaldo
- F. Roosen‐Runge
- Gustavo D. Parisi
- Fajun Zhang
- Tadeo E. Saldaño
- L. Looger
- Frank Schreiber
In Spectroscopy
Citations in the corpus
- Structured states of disordered proteins from genomic sequences (2016, neutral): “, 1963; Perutz, 1970) and is associated with diverse cellular functions including metabolism, gene regulation, signaling, and molecular transport, spurring growing interest in so-called disordered and low-complexity sequences (Bah et al., 2015; Ferreon et al., 2013; Motlagh et al., 2014; Tokuriki an”
- Impact of protein conformational diversity on AlphaFold predictions (2021, background): “These differences are also relevant for signal transduction [16] and define metabolic regulation by mechanisms like cooperativity and allosterism [10,17–19].”
- Extant fold-switching proteins are widespread (2018, background): “Accordingly, changes in the cellular environment are thought to favor globular protein conformations whose functional capacities differ (4) because of localized structural variations on an essentially unchanged framework of anchoring secondary structure (3), although some solvent-exposed secondary s”
- Designing allostery-inspired response in mechanical networks (2016, background): “Statistical fluctuations in the structure of proteins have been shown to play an important role in allosteric functionality (22, 23).”
- Dynamics of proteins in solution (2019, background): “For further reading on this topic, we refer the reader to Kern and Zuiderweg (2003); Tzeng and Kalodimos (2011); Motlagh et al. (2014); Kornev and Taylor (2015); Papaleo et al. (2016).”