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Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 20, Zeilen: 1-13
Quelle: Wikipedia Serine-threonine-specific protein kinase 2006
Seite(n): 1 (online source), Zeilen: -
Structure and autoregulation

The CaM kinases consist of an N-terminal catalytic domain, a regulatory domain and an associative domain. In the absence of Ca2+/calmodulin, the catalytic domain is auto inhibited by the regulatory domain, which contains a pseudo substrate sequence. Several CaM kinases aggregate into a homo-oligomer or hetero-oligomer. Upon activation by Ca2+/calmodulin, the activated CaM kinases autophosphorylate each other, in an intermolecular reaction.

This has two effects:

• An increase in affinity for the calmodulin complex, prolonging the time the kinase is active.

• Continued activation of the phosphorylated kinase complex even after the calmodulin complex has dissociated from the kinase complex, which prolongs the active state even more.

Structure and autoregulation

The CaM kinases consist of an N-terminal catalytic domain, a regulatory domain, and an association domain. In the absence of Ca2+/calmodulin, the catalytic domain is autoinhibited by the regulatory domain, which contains a pseudosubstrate sequence. Several CaM kinases aggregate into a homooligomer or heterooligomer. Upon activation by Ca2+/calmodulin, the activated CaM kinases autophosphorylate each other in an intermolecular reaction. This has two effects:

1. An increase in affinity for the calmodulin complex, prolonging the time the kinase is active.

2. Continued activation of the phosphorylated kinase complex even after the calmodulin complex has dissociated from the kinase complex, which prolongs the active state even more.

Anmerkungen

No source is given.

Sichter
(Hindemith), WiseWoman

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