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Related Concept Videos

Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
Interaction domains in cell signaling
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Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Allosteric Regulation01:08

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

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Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET
10:59

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Published on: August 17, 2022

Allosteric conformational barcodes direct signaling in the cell.

Ruth Nussinov1, Buyong Ma, Chung-Jung Tsai

  • 1Basic Science Program, SAIC-Frederick, Inc., Cancer and Inflammation Program, National Cancer Institute, Frederick, MD 21702, USA; Sackler Institute of Molecular Medicine, Department of Human Genetics and Molecular Medicine, Sackler School of Medicine, Tel Aviv University, Tel Aviv 69978, Israel.

Structure (London, England : 1993)
|September 10, 2013
PubMed
Summary

Cellular pathways are controlled by unique conformational barcodes on proteins. These structural signals dictate pathway direction, influencing cell fate, proliferation, and death.

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Area of Science:

  • Cellular Biology
  • Biochemistry
  • Structural Biology

Background:

  • Cellular networks feature complex, interconnected pathways that merge, diverge, and share components.
  • Understanding the control mechanisms and directionality of these pathways is crucial, especially for signaling pathways regulating fundamental cellular processes like fate, proliferation, and death.
  • A limited set of core pathways are extensively utilized in biological regulation.

Purpose of the Study:

  • To review the structural basis for cellular pathway control and directionality.
  • To explore how allosteric events collectively encode information within protein structures.
  • To elucidate the mechanism by which structural information dictates cellular responses.

Main Methods:

  • Literature review focusing on the structural standpoint of cellular signaling.
  • Analysis of how co-occurring allosteric events contribute to protein functional site "barcoding."
  • Examination of the role of conformational barcodes in signal transmission and partner selection.

Main Results:

  • Allosteric events, including posttranslational modifications and mutations, create unique conformational barcodes at protein functional sites.
  • These barcodes act as intracellular address labels, selectively mediating interactions.
  • The shape of the conformational barcode determines binding specificity, thereby directing pathway flow.

Conclusions:

  • Conformational barcodes are key determinants of cellular pathway directionality.
  • These structural codes regulate signal transmission, influencing cell fate, proliferation, and death.
  • Understanding these mechanisms provides insight into the intricate regulation of cellular processes.