The Structural Bases of CDK5 Activity View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2008-06-30

AUTHORS

Andrea Musacchio

ABSTRACT

In the last 15 years, a wealth of structural investigations on protein kinases has been reported. These studies have revealed that the active states of protein kinases are usually structurally alike, a requirement imposed by the necessity to maintain the basic geometry of a highly conserved machinery required for good catalytic output. Conversely, the structures of the inactive states of kinase-family members can vary widely from each other, a principle that can be exploited to improve the specificity of kinase inhibitors. In this chapter, we discuss the activation mechanism of the CDK5 kinase within the general frame of reference of kinase activation mechanisms, and in comparison to other members of the CDK family. We explain how CDK5, not unlike other kinases, has made its own capricious decisions to design an original activation mechanism and distinguish itself from CDK-family relatives. More... »

PAGES

191-210

Book

TITLE

Cyclin Dependent Kinase 5 (Cdk5)

ISBN

978-0-387-78886-9
978-0-387-78887-6

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-0-387-78887-6_14

DOI

http://dx.doi.org/10.1007/978-0-387-78887-6_14

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1027467036


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