Structure-based model of allostery predicts coupling between distant sites

Allostery is a phenomenon that couples effector ligand binding at an allosteric site to a structural and/or dynamic change at a distant regulated site. To study an allosteric transition, we vary the size of the allosteric site and its interactions to construct a series of energy landscapes with pron...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2012-03, Vol.109 (13), p.4875-4880
Hauptverfasser:	Weinkam, Patrick, Pons, Jaume, Sali, Andrej
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric Regulation Allosteric Site binding proteins Binding sites Biological Sciences Calcium Calcium - metabolism chemistry Crystal structure Energy Entropy Fluorescence Green Fluorescent Proteins Green Fluorescent Proteins - chemistry Green Fluorescent Proteins - metabolism landscapes Ligands Maltose-Binding Proteins Maltose-Binding Proteins - chemistry Maltose-Binding Proteins - metabolism Mathematical minima metabolism Modeling Models, Molecular Molecular dynamics Protein Structure, Secondary Proteins Structure-Activity Relationship transcription factors Transcription Factors - chemistry Transcription Factors - metabolism
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