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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...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Enzyme-linked Receptors01:00

Enzyme-linked Receptors

Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
Neurotrophin (NT) receptors are a family of RTKs, including trkA, trkB, and trkC (tropomyosin-related kinase) receptors. TrkA is specific for nerve growth factor (NGF), neurotrophin-6, and neurotrophin-7. TrkB binds...
Spare Receptors01:30

Spare Receptors

Some receptors remain unoccupied even when an agonist produces a maximal response. Such empty ones are called spare receptors. In presence of spare receptors the maximum effect of an agonist drug is achieved with fewer than 100% of the receptors being occupied. To determine the presence of spare receptors, scientists often compare the concentration of the drug needed to produce 50% of the maximum effect (EC50) with the concentration of the drug needed to occupy 50% of the receptors (Kd). If the...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
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Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
16:16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

RAGE: a single receptor fits multiple ligands.

Günter Fritz1

  • 1University of Freiburg, Department of Neuropathology, Neurozentrum, Breisacher Str. 64 79106 Freiburg, Germany. guenter.fritz@uniklink-freiburg.de

Trends in Biochemical Sciences
|October 25, 2011
PubMed
Summary
This summary is machine-generated.

The receptor for advanced glycation end products (RAGE) recognizes diverse ligands through electrostatic interactions. This study proposes a mechanism for RAGE

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Area of Science:

  • Immunology
  • Structural Biology
  • Biochemistry

Background:

  • The receptor for advanced glycation end products (RAGE) is a key signaling molecule in innate immunity and inflammation.
  • RAGE is a pattern recognition receptor, binding diverse ligands based on shared features rather than specific molecular identity.

Purpose of the Study:

  • To elucidate the mechanism behind RAGE's broad ligand recognition.
  • To propose a model for RAGE ligand binding and subsequent receptor activation.

Main Methods:

  • Analysis of recent X-ray crystallographic and NMR structural data of the RAGE ectodomain.
  • Integration of biochemical data concerning RAGE-ligand interactions.

Main Results:

  • Structural data reveal a positively charged surface on the RAGE ectodomain.
  • Ligand binding is primarily mediated by electrostatic interactions between RAGE and negatively charged ligands.

Conclusions:

  • A putative mechanism for RAGE's unusual ligand recognition and activation is proposed.
  • Electrostatic interactions are central to RAGE's role in innate immunity and inflammation.