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Related Concept Videos

Receptor Tyrosine Kinases01:26

Receptor Tyrosine Kinases

Receptor tyrosine kinases or RTKs are membrane-bound receptors that phosphorylate specific tyrosine on protein substrates. RTKs regulate cellular growth, differentiation, survival, and migration. They contain an extracellular ligand binding domain, a transmembrane domain, and a cytosolic tail with intrinsic kinase activity. Several extracellular signaling molecules activate RTKs in one or more ways and relay the signal downstream. Ligands such as platelet-derived growth factor (PDGF) or...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
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...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...

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Related Experiment Video

Updated: Jun 16, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
06:45

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay

Published on: May 26, 2011

Receptor tyrosine kinase transmembrane domains: Function, dimer structure and dimerization energetics.

Edwin Li1, Kalina Hristova

  • 1Department of Materials Science and Engineering, Johns Hopkins University, Baltimore, MD, USA.

Cell Adhesion & Migration
|February 20, 2010
PubMed
Summary

Transmembrane domains of receptor tyrosine kinases (RTKs) are crucial for signaling stability. New structural insights reveal their role in receptor dimerization and signaling competence, advancing the field.

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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Transmembrane (TM) domains of receptor tyrosine kinases (RTKs) are integral to cellular signaling.
  • These domains stabilize receptor dimers and maintain a signaling-ready conformation.
  • Understanding RTK TM domain function is key to deciphering cell communication.

Purpose of the Study:

  • To review newly solved structures of RTK TM domains.
  • To discuss the energetics of RTK TM domain dimerization.
  • To explore the impact of mutations on RTK TM domain structure and dimerization.

Main Methods:

  • Structural biology techniques (e.g., X-ray crystallography, cryo-EM) were used to solve RTK TM domain structures.
  • Biophysical methods were employed to study dimerization energetics.
  • Analysis of pathogenic mutations in RTK TM domains.

Main Results:

  • Two novel structures of RTK TM domains have been determined.
  • Recent studies provide insights into RTK TM domain dimerization energetics.
  • The effects of pathogenic mutations on RTK TM domain structure and dimerization are being investigated.

Conclusions:

  • The solved structures represent a breakthrough in understanding RTK TM domain function.
  • RTK TM domains actively contribute to receptor stability and signaling.
  • Further research on RTK TM domains, including mutation effects, is essential for understanding RTK signaling.