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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...
Cell-surface Signaling01:21

Cell-surface Signaling

Hormones—or any molecule that binds to a receptor, known as a ligand—that are lipid-insoluble (water-soluble) are not able to diffuse across the cell membrane. In order to be able to affect a cell without entering it, these hormones bind to receptors on the cell membrane. When a first messenger, a hormone, binds to a receptor, a signal cascade is set off, causing second messengers, proteins inside the cell, to become activated, resulting in downstream effects.
Hedgehog Signaling Pathway02:33

Hedgehog Signaling Pathway

The Hedgehog gene (Hh) was first discovered due to its control of the growth of disorganized, hair-like bristles phenotype in Drosophila, much like hedgehog spines. Hh plays a crucial role in the development of organs and the maintenance of homeostasis in both invertebrates and vertebrates. However, while Drosophila has only one Hh protein, mammals have multiple functional Hedgehog proteins - Sonic (Shh), Desert (Dhh), and Indian Hedgehog (Ihh). All of these homologous proteins have adapted to...
Hedgehog Signaling Pathway02:33

Hedgehog Signaling Pathway

The Hedgehog gene (Hh) was first discovered due to its control of the growth of disorganized, hair-like bristles phenotype in Drosophila, much like hedgehog spines. Hh plays a crucial role in the development of organs and the maintenance of homeostasis in both invertebrates and vertebrates. However, while Drosophila has only one Hh protein, mammals have multiple functional Hedgehog proteins - Sonic (Shh), Desert (Dhh), and Indian Hedgehog (Ihh). All of these homologous proteins have adapted to...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...

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Related Experiment Video

Updated: Jul 16, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
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Published on: September 11, 2015

The EGF receptor Hokey-Cokey.

Dan Niculescu-Duvaz1, Steven Whittaker, Caroline Springer

  • 1The Institute of Cancer Research, Gene and Oncogene Targeting Team, Cancer Research UK Centre for Cancer Therapeutics, Sutton, Surrey SM2 5NG, UK.

Cancer Cell
|March 14, 2007
PubMed
Summary

Structural insights into epidermal growth factor receptor (EGFR) activation reveal how mutations and drug binding stabilize active or inactive states. This research aids in developing targeted anti-EGFR cancer therapies.

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Last Updated: Jul 16, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
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Published on: September 11, 2015

Validated Immunochemical Assay for Comprehensive Determination of the Human Epidermal Growth Factor Receptor 2 Released from and Bound to Cells
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Area of Science:

  • Oncology
  • Structural Biology
  • Pharmacology

Background:

  • Epidermal growth factor receptor (EGFR) mutations drive cancer by promoting an active conformation.
  • Small-molecule drugs targeting EGFR can bind to its inactive or active states.

Purpose of the Study:

  • To elucidate the structural basis of EGFR activation and drug binding.
  • To provide insights for developing novel anti-EGFR therapeutics.

Main Methods:

  • X-ray crystallography was used to determine 12 structures.
  • Structures included wild-type and mutant EGFR kinase domains bound to four distinct ligands.

Main Results:

  • Detailed structural information on EGFR kinase domain conformations.
  • Visualizations of drug interactions with both active and inactive EGFR states.

Conclusions:

  • The presented structures offer a valuable resource for rational drug design.
  • Understanding EGFR conformational dynamics is key for effective cancer treatment development.