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![[Figure 1]](ba5290fig1mag.jpg)
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Figure 1
Protein energy landscapes and allostery. (a) A generic framework for allostery is that the global energy landscape of the protein is altered by an allosteric effector. Here, the energy landscape is schematized as a plot of free energy versus an arbitrary collective conformational coordinate. An allosteric effector, here a small-molecule ligand binding at an allosteric site, modulates the energy landscape, which changes the conformation of the active site (*), thus altering the function of the protein. (b) However, the portrait in (a) is agnostic to the mechanisms by which the local energy landscapes of specific regions of a protein structure respond to the allosteric effector and to each other. It therefore remains unclear how the allosteric signal propagates from the allosteric site through the tertiary structure to the functional site. Although this propagation may be branching rather than linear as depicted schematically here, it must ultimately have a physical mechanistic basis that can be understood in structural terms. |
![[Figure 1]](ba5290fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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