Induced fit

From Proteopedia

Jump to: navigation, search
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

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

Personal tools