Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
Drugs Affecting GI Tract Motility: Serotonin Receptor Agonists01:23

Drugs Affecting GI Tract Motility: Serotonin Receptor Agonists

Serotonin, a crucial neurotransmitter synthesized by enterochromaffin cells, plays a cardinal role in regulating gastrointestinal (GI) motility. With over 90% of the body's total serotonin in the GI tract, its influence on digestive processes is profound. Serotonin is swiftly released upon various stimuli, such as food boluses or certain drugs, triggering intrinsic sensory neurons in the myenteric plexus and extrinsic vagal and spinal sensory neurons. This leads to the activation of 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...
Adrenergic Agonists: Chemistry and Structure-Activity Relationship01:16

Adrenergic Agonists: Chemistry and Structure-Activity Relationship

Adrenergic agonists' structure-activity relationship (SAR) determines their selectivity and efficacy. These agonists comprise a phenylethylamine moiety with an aromatic ring and an ethylamine side chain.
Aromatic ring substitutions: Substituting the aromatic ring with –OH groups at positions 3 and 4 yields catecholamines (e.g., epinephrine), which have a high affinity for adrenoceptors. Hydrogen bonding between –OH groups and receptors enhances adrenergic activity.
Separation of the aromatic...
Olfactory Receptors: Location and Structure01:03

Olfactory Receptors: Location and Structure

The process of olfaction, also known as the sense of smell, is a sophisticated chemical response system. The specialized sensory neurons that facilitate this process, known as olfactory receptor neurons, are situated in an upper segment of the nasal cavity, known as the olfactory epithelium. Olfactory sensory neurons are bipolar, with their dendrites extending from the epithelium's apex into the mucus that lines the nasal cavity. Airborne molecules, when inhaled, traverse the olfactory...
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
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

No evidence for direct physical interaction of 5-HT <sub>2A</sub> -mGluR2 receptors <i>in vitro</i> or <i>in vivo</i>.

bioRxiv : the preprint server for biology·2026
Same author

GPCR Biased Signaling: Opportunities and Challenges.

Biochemistry·2026
Same author

Structural characterization of kappa-opioid receptor dimer in complex with two G proteins.

Nature communications·2026
Same author

Toward a Random Background for Ligand Optimization.

bioRxiv : the preprint server for biology·2026
Same author

De novo design of miniproteins targeting GPCRs.

Nature·2026
Same author

The Selectivity Implications of Docking Libraries with Greater and Lesser Similarities to Bio-like Molecules.

Journal of medicinal chemistry·2026

Related Experiment Video

Updated: May 13, 2026

Rapid In Situ Hybridization using Oligonucleotide Probes on Paraformaldehyde-prefixed Brain of Rats with Serotonin Syndrome
08:49

Rapid In Situ Hybridization using Oligonucleotide Probes on Paraformaldehyde-prefixed Brain of Rats with Serotonin Syndrome

Published on: September 23, 2015

Structural basis for molecular recognition at serotonin receptors.

Chong Wang1, Yi Jiang, Jinming Ma

  • 1Department of Integrative Structural and Computational Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.

Science (New York, N.Y.)
|March 23, 2013
PubMed
Summary

Crystal structures reveal how serotonin 5-HT1B receptor binds antimigraine drugs. This clarifies drug action and aids in designing new, selective serotonergic medications.

More Related Videos

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
12:21

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

Published on: November 27, 2016

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination
11:24

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination

Published on: May 13, 2017

Related Experiment Videos

Last Updated: May 13, 2026

Rapid In Situ Hybridization using Oligonucleotide Probes on Paraformaldehyde-prefixed Brain of Rats with Serotonin Syndrome
08:49

Rapid In Situ Hybridization using Oligonucleotide Probes on Paraformaldehyde-prefixed Brain of Rats with Serotonin Syndrome

Published on: September 23, 2015

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram
12:21

Thermostabilization, Expression, Purification, and Crystallization of the Human Serotonin Transporter Bound to S-citalopram

Published on: November 27, 2016

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination
11:24

High Precision FRET at Single-molecule Level for Biomolecule Structure Determination

Published on: May 13, 2017

Area of Science:

  • Neuroscience
  • Pharmacology
  • Structural Biology

Background:

  • Serotonin (5-hydroxytryptamine, 5-HT) is a key neurotransmitter regulating diverse physiological functions via its receptor family.
  • The 5-HT receptor family, particularly the 5-HT1B subtype, is a target for therapeutic interventions, including antimigraine medications.

Purpose of the Study:

  • To elucidate the structural basis of ligand binding to the human 5-HT1B G protein-coupled receptor (GPCR).
  • To understand the molecular interactions of ergotamine and dihydroergotamine with the 5-HT1B receptor.
  • To provide insights for the rational design of subtype-selective serotonergic drugs.

Main Methods:

  • X-ray crystallography to determine the structures of the 5-HT1B receptor bound to ergotamine and dihydroergotamine.
  • Molecular docking simulations.
  • Site-directed mutagenesis studies.

Main Results:

  • The crystal structures reveal conserved binding modes of ergotamine and dihydroergotamine within the 5-HT1B receptor's orthosteric and extended pockets.
  • Key residues forming the orthosteric pocket are conserved across the 5-HT receptor family, explaining broad agonist activity.
  • A distinct outward shift in helix V of the 5-HT1B receptor compared to the 5-HT2B receptor creates a more open extended pocket, contributing to subtype selectivity.

Conclusions:

  • The determined structures offer a detailed molecular understanding of 5-HT1B receptor activation by ergotamine and dihydroergotamine.
  • These findings provide a structural foundation for developing novel drugs targeting the 5-HT1B receptor with improved selectivity and efficacy.
  • The study highlights the importance of structural insights in advancing the field of serotonergic drug discovery.