Strukturbiologie der humanen PIM-1-Kinase

The protein PIM-1 is a serine/threonine kinase which is expressed of the gene pim-1. pim-1 is a proto-oncogene which is implicated in molecular mechanisms of differentiating and proliferation. The cristallography allows to determine the structures of macromolecules. For this the protein kinase PIM-1 has been expressed in E.coli, purified, and found in different phosphorylation forms. These phosphorylations forms were differentiated in three main peaks by the Anionic Exchange Column of Amersham Pharmacia, MonoQ HR 10/10, controlled by the NaCl-gradient. Most kinases are regulated by the phosphorylation of their variable loop. But there exist other kinases which are constitutive active. This means for their activity the phosphorylation is not necessary. Kinase assays carried out by Gruenenthal GmbH showed that all phosphorylation forms of PIM-1 have similar kinase activities. This means PIM-1 is regulated by another mechanism than phosphorylation. For example by the expression and translation of its gene pim-1, by intramolecular interactions between the loops and its degradation by the proteasom. Most of the kinase inhibitors are designed to the ATP pocket because this location is in all eucaryotic protein kinases highly conserved.

Grantor dc:publisher

Publikationsserver der RWTH Aachen University

Year dc:date

2006

Author dc:creator

• Betz, Katja

Contributors dc:contributor

• Fischer, Rainer

• info:eu-repo/classification/ddc/570
• Biowissenschaften, Biologie

Statement dc:rights

• info:eu-repo/semantics/openAccess

Language dc:language

ger

Identifier

https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114782%22

OAI record oai:identifier

https://publications.rwth-aachen.de/oai2d?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Apublications.rwth-aachen.de%3A52567