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Induced fit

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This is a [[morphs|morph]] of the <scene name='31/318562/Hexokinase/3'>closed and open form of hexokinase</scene> (be patient when loading this). The first and the last frame of the animation are models based on crystallographic data while the intermediate states are somewhat arbitrary, but chosen to show a smooth transition between conformations.
This is a [[morphs|morph]] of the <scene name='31/318562/Hexokinase/3'>closed and open form of hexokinase</scene> (be patient when loading this). The first and the last frame of the animation are models based on crystallographic data while the intermediate states are somewhat arbitrary, but chosen to show a smooth transition between conformations.
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<text>Closed</text>
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Revision as of 17:28, 13 April 2021

Morph of hexokinase in the open 3o80 and glucose-bound closed 3o8m 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.
Morph of hexokinase in the open 3o80 and glucose-bound closed 3o8m 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.

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 classic example of induced fit is binding of glucose to hexokinase, depicted in a morph between 3o8m and 3o80 in the picture at right.


Contents

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

Drag the structure with the mouse to rotate

See Also


References

  1. ↑ doi: https://dx.doi.org/10.1002/anie.199423751
  2. ↑ doi: https://dx.doi.org/10.1002/cber.18940270364

Proteopedia Page Contributors and Editors (what is this?)

Karsten Theis, Eric Martz, Eran Hodis

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