Allostery in the dynamic coactivator domain KIX occurs through minor conformational micro-states

The coactivator KIX of CBP uses two binding surfaces to recognize multiple activators and exhibits allostery in ternary complex formation. Activator•coactivator interactions are central to transcriptional regulation, yet the microscopic origins of allostery in dynamic proteins like KIX are largely u...

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Veröffentlicht in:	PLoS computational biology 2022-04, Vol.18 (4), p.e1009977-e1009977
Hauptverfasser:	Peiffer, Amanda L, Garlick, Julie M, Joy, Stephen T, Mapp, Anna K, Brooks, 3rd, Charles L
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric properties Allosteric proteins Binding Binding Sites Biology and Life Sciences Biometric recognition systems c-Myb protein Chain dynamics Clustering Complex formation CREB-Binding Protein - chemistry CREB-Binding Protein - metabolism Crystal structure Entropy Fluorimetry Gene regulation Ligands Molecular Conformation Molecular dynamics Molecular Dynamics Simulation Mutation Order parameters Physical Sciences Physiological aspects Protein Binding Proteins Research and Analysis Methods Simulation Ternary systems Transcription factors Transcriptional coactivators
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