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Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 20, Zeilen: 14-40
Quelle: Wikipedia Protein kinase 2007
Seite(n): 1 (online source), Zeilen: -
2) Tyrosine-specific protein kinases

Tyrosine-specific protein kinases phosphorylate tyrosine amino acid residues, and are, like serine/threonine-specific kinases, used in signal transduction. They act primarily as growth factor receptors and in downstream signaling from growth factors; some examples:

• Platelet-derived growth factor (PDGF) receptor;

• Epidermal growth factor (EGF) receptor;

• Insulin receptor and insulin-like growth factor (IGF1) receptor;

• Stem cell factor (scf) receptor (also called c-kit).

- Receptor tyrosine kinases:

These kinases consist of a transmembrane receptor with a tyrosine kinase domain protruding into the cytoplasm. They play an important role in regulating cell division, cellular differentiation, and morphogenesis. More than 50 receptor tyrosine kinases are known in mammals.

Structure

The extracellular domain serves as the ligand-binding part of the molecule. It can be a separate unit that is attached to the rest of the receptor by a disulfide bond. The same mechanism can be used to bind two receptors together to form a homo- or heterodimer. The transmembrane element is a single α helix. The intracellular or cytoplasmic domain is responsible for the (highly conserved) kinase activity, as well as several regulatory functions.

Regulation

Ligand binding causes two reactions:

• dimerization of two monomeric receptor kinases or

• stabilization of a loose dimer.

Many ligands of receptor tyrosine kinases are multivalent. Some tyrosine receptor kinases (e.g., the platelet-derived growth factor receptor) can form heterodimers with other similar but not identical kinases of the same subfamily, allowing a highly varied response to the extracellular signal.

Tyrosine-specific protein kinases

[...]

Tyrosine-specific protein kinases (EC 2.7.10.1) phosphorylate tyrosine amino acid residues, and are, like serine/threonine-specific kinases, used in signal transduction. They act primarily as growth factor receptors and in downstream signaling from growth factors; some examples:

• Platelet-derived growth factor (PDGF) receptor;

• Epidermal growth factor (EGF) receptor;

• Insulin receptor and insulin-like growth factor (IGF1) receptor;

• Stem cell factor (scf) receptor (also called c-kit, see the article on gastrointestinal stromal tumor).

Receptor tyrosine kinases

These kinases consist of a transmembrane receptor with a tyrosine kinase domain protruding into the cytoplasm. They play an important role in regulating cell division, cellular differentiation, and morphogenesis. More than 50 receptor tyrosine kinases are known in mammals.

Structure

The extracellular domain serves as the ligand-binding part of the molecule. It can be a separate unit that is attached to the rest of the receptor by a disulfide bond. The same mechanism can be used to bind two receptors together to form a homo- or heterodimer. The transmembrane element is a single α helix. The intracellular or cytoplasmic domain is responsible for the (highly conserved) kinase activity, as well as several regulatory functions.

Regulation

Ligand binding causes two reactions:

1. Dimerization of two monomeric receptor kinases or stabilization of a loose dimer. Many ligands of receptor tyrosine kinases are multivalent. Some tyrosine receptor kinases (e.g., the platelet-derived growth factor receptor) can form heterodimers with other similar but not identical kinases of the same subfamily, allowing a highly varied response to the extracellular signal.

Anmerkungen

No source is given.

The bullet points under Regulation are misleading, as the two reactions are the one on the bottom of page 20 and the one on the top of page 21.

Sichter
(Hindemith), WiseWoman

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