INTRODUCTION :

Enzyme-linked receptor proteins either possess an

in-built enzyme or associate with separate enzymes
in the cytoplasm.
These enzymes are activated upon ligand binding.
They relay the extracellular signal to the nucleus by
a sequence of interactions that eventually turn on
specific transcription factors, altering gene
expression in the cell.



Basic receptor structure
All enzyme-linked receptors share a few
common features;

1. Ligand-binding domain

Extracellular to allow easy access for ligands.
Strong affinity for specific ligands - allows
different ligands that bind to the same
receptor to evoke particular cellular
responses.

2. Transmembrane domain

Contains a series of hydrophobic amino acids.
Tethers the receptor to the cell membrane.


3. Cytosolic "active" enzyme domain

Either intrinsic to the receptor or tightly bound
via the cytosolic domain.
The majority are kinases; they phosphorylate
specific threonine, serine, and tyrosine amino
acid residues (THR,S,TY = THIRSTY).


There are three main types of enzyme-linked
receptors:

1. Receptor serine-threonine kinases e.g.
transforming growth factor-beta (TGFB)
receptors.

2. Receptor tyrosine kinases (RTKs) e.g. growth
factor receptors.

3. Tyrosine-kinase-associated receptors e.g.
cytokine receptors
1. Receptor serine/threonine kinases
2. Receptor tyrosine kinases (RTKs)
3. Tyrosine-kinase-associated receptors

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