The modular logic of signaling proteins: building allosteric switches from simple binding domains.
Many eukaryotic signal transduction proteins have component-based architectures: they are built from combinations of protein interaction domains and catalytic domains. Intact, these proteins display the sophisticated allosteric behavior required for cellular regulation; the protein's output activity is tightly repressed under basal conditions, but can be robustly activated by a specific set of input effector ligands. A combination of structural, biophysical and computational studies is beginning to shed light on the fundamental principles governing this type of modular allostery.
Lim
Wendell A
WA
Department of Cellular and Molecular Pharmacology, Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0450, USA. wlim@itsa.ucsf.edu
D000494:Allosteric Regulation / Q000502:physiology; D000495:Allosteric Site / Q000502:physiology; D000818:Animals; D001665:Binding Sites / Q000502:physiology; D006801:Humans; D008024:Ligands; D011487:Protein Conformation; D017434:Protein Structure, Tertiary / Q000502:physiology; D011506:Proteins / Q000737:chemistry / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D013816:Thermodynamics; D051316:Wiskott-Aldrich Syndrome Protein; D019061:src-Family Kinases / Q000737:chemistry / Q000502:physiology
D008024:Ligands; D011506:Proteins; C495767:WAS protein, human; D051316:Wiskott-Aldrich Syndrome Protein; D019061:src-Family Kinases