Induced fit
From Proteopedia
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[[Induced fit]] describes a conformational change in a protein when it binds a ligand, in contrast to a lock-and-key model of ligand binding. A classical example of induced fit is binding of glucose to hexokinase, depicted in a morph between [[3o8m]] and [[3o80]] below. | [[Induced fit]] describes a conformational change in a protein when it binds a ligand, in contrast to a lock-and-key model of ligand binding. A classical example of induced fit is binding of glucose to hexokinase, depicted in a morph between [[3o8m]] and [[3o80]] below. | ||
| - | [[Image:Induced fit.gif]] | + | [[Image:Induced fit.gif|frame|Morph of hexokinase in the open [[3o8m]] and glucose-boudn closed [[3o80]] conformation. For reference, glucose (purple) is shown throughout the morph. Two views are shown, an overview as spacefill and a detail of the binding site in wireframe.]] |
==History of the concept== | ==History of the concept== | ||
Revision as of 15:34, 13 April 2021
Induced fit describes a conformational change in a protein when it binds a ligand, in contrast to a lock-and-key model of ligand binding. A classical example of induced fit is binding of glucose to hexokinase, depicted in a morph between 3o8m and 3o80 below.
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History of the concept
Induced fit was suggested by Koshland in 1958 [1], providing an alternative to the lock-and-key binding model that Emil Fischer proposed in 1899 [2].
Interactive examples
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See Also
- A morph of induced fit when Tamiflu binds to Neuraminidase.
