Allostery without a conformational change? Revisiting the paradigm

Ruth Nussinov*, Chung Jung Tsai

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review


Classically, allostery induces a functional switch through a conformational change. However, lately an increasing number of studies concluded that the allostery they observe takes place through sheer dynamics. Here we explain that even if a structural comparison between the active and inactive states does not detect a conformational change, it does not mean that there is no conformational change. We list likely reasons for this lack of observation, including crystallization conditions and crystal effects; one of the states is disordered; the structural comparisons disregard the quaternary protein structure; overlooking synergy effects among allosteric effectors and graded incremental switches and too short molecular dynamics simulations. Specific functions are performed by distinct conformations; they emerge through specific interactions between conformationally selected states.

Original languageEnglish
Pages (from-to)17-24
Number of pages8
JournalCurrent Opinion in Structural Biology
StatePublished - 1 Feb 2015


FundersFunder number
Center for Cancer Research
National Institutes of HealthHHSN261200800001E
National Cancer InstituteZIABC010442


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