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Related Concept Videos

The Two-State Receptor Model01:29

The Two-State Receptor Model

The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
The binding affinity of a drug determines its interaction with one...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
Activation and Inactivation of G Proteins01:22

Activation and Inactivation of G Proteins

Heterotrimeric G proteins are guanine nucleotide-binding proteins. As the name suggests, heterotrimeric G proteins are composed of three subunits: alpha, beta, and gamma. They remain GDP-bound or GTP-bound inside the cells and switch between inactive/active states. The Gα subunit possesses the nucleotide-binding pocket that binds guanine nucleotides and switches between GDP or GTP-bound states. In contrast, the Gꞵ and Gγ subunits are always bound together with high affinity and are together...
RNA Polymerase II Accessory Proteins02:36

RNA Polymerase II Accessory Proteins

Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
Assembly of Signaling Complexes01:30

Assembly of Signaling Complexes

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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tRNA Activation

Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...

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Related Experiment Video

Updated: May 17, 2026

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
12:43

Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE

Published on: July 29, 2014

A structure-based model of RIG-I activation.

Daniel Kolakofsky1, Eva Kowalinski, Stephen Cusack

  • 1Department of Microbiology and Molecular Medicine, University of Geneva School of Medicine, CMU, 1211 Geneva, Switzerland. daniel.kolakofsky@unige.ch

RNA (New York, N.Y.)
|November 3, 2012
PubMed
Summary
This summary is machine-generated.

Recent crystal structures reveal how Retinoic acid-inducible gene I (RIG-I) activates upon binding viral RNA. This provides key insights into innate immune receptor activation mechanisms against viral infections.

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Monitoring Activation of the Antiviral Pattern Recognition Receptors RIG-I And PKR By Limited Protease Digestion and Native PAGE
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Published on: July 29, 2014

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Published on: May 20, 2020

Area of Science:

  • Structural Biology
  • Immunology
  • Virology

Background:

  • The innate immune system relies on pattern recognition receptors (PRRs) to detect pathogen-associated molecular patterns.
  • Retinoic acid-inducible gene I (RIG-I) is a crucial PRR that senses viral RNA, initiating antiviral immune responses.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying RIG-I activation by viral RNA.
  • To provide atomic-level insights into the interaction between RIG-I and its cognate ligands.

Main Methods:

  • High-resolution crystal structure determination of RIG-I.
  • Co-crystallization of RIG-I with double-stranded RNA (dsRNA).
  • Comparative structural analysis of different RIG-I:dsRNA complexes.

Main Results:

  • Detailed structural snapshots of RIG-I in both apo and RNA-bound states were obtained.
  • Key conformational changes in RIG-I upon dsRNA binding were identified.
  • The structural basis for RIG-I's specificity towards certain viral RNA structures was revealed.

Conclusions:

  • The reported crystal structures offer significant insights into the activation mechanism of RIG-I.
  • Understanding RIG-I activation is critical for developing novel antiviral therapies targeting innate immunity.