Dynamic activation of an allosteric regulatory protein

378 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Structures of inactive CRP species reveal the atomic details of the allosteric transition that discriminates cyclic nucleotide second messengers. (2014, background): “…of protein dynamics, allosteric transitions are often described as an equilibrium shift of the pre-existing activestate and inactive-state populations based on a conformational selection theory of stabilization of the active state by the allosteric effector (Tzeng & Kalodimos, 2009, 2012, 2013).”
Induced fit, conformational selection and independent dynamic segments: an extended view of binding events (2010, neutral): “High affinity binding typically requires additional adjustment step; this step could be a general increase in protein dynamism at the binding site after specific binding has already been established [64] or conversely, a rigidification of the IDP partner [53].”
The Crystal Structures of Apo and cAMP-Bound GlxR from Corynebacterium glutamicum Reveal Structural and Dynamic Changes upon cAMP Binding in CRP/FNR Family Transcription Factors (2014, background): “The two binding events are thus highly correlated leading to large changes in dynamic behavior supporting the notion of a largely dynamically driven process of allostery [47].”
Dynamic Fluctuations Provide the Basis of a Conformational Switch Mechanism in Apo Cyclic AMP Receptor Protein (2013, background): “mechanism in play [20,23].”