Architecture and activation of phosphatidylinositol 3-kinase related kinases
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 4449455
Author(s) Imseng, Stefan; Aylett, Christopher Hs; Maier, Timm
Author(s) at UniBasel Maier, Timm
Year 2018
Title Architecture and activation of phosphatidylinositol 3-kinase related kinases
Journal Current opinion in structural biology
Volume 49
Pages / Article-Number 177-189
Mesh terms Chromatin, chemistry; Humans; Models, Molecular; Phosphatidylinositol 3-Kinase, metabolism; Protein Binding; Protein Conformation; Protein Interaction Domains and Motifs; Protein Kinases, metabolism; Protein Multimerization; Protein Subunits; Repetitive Sequences, Amino Acid; Sirolimus, chemistry; Structure-Activity Relationship; TOR Serine-Threonine Kinases, metabolism
Abstract The phosphatidylinositol 3-kinase related protein kinases (PIKKs) are key to the regulation of a variety of eukaryotic cellular processes including DNA repair and growth regulation. While these massive proteins had long resisted structural analysis, recent advances in electron cryo-microscopy have now facilitated structural analysis of the major examples of PIKKs, including mTOR, DNA-PK, ATM, ATR and TRAPP/Tra1. In these PIKKs, the carboxy-terminal kinase domains and their proximal regions are structurally conserved. The structural organization of their extensive amino-terminal repeat regions, however, as well as their oligomeric organization and their interactions with accessory proteins, differ markedly amongst PIKKs. This architectural divergence provides the structural basis for the complex regulatory roles and functional diversity of PIKKs.
Publisher CURRENT BIOLOGY LTD
ISSN/ISBN 1879-033X
edoc-URL https://edoc.unibas.ch/63415/
Full Text on edoc No
Digital Object Identifier DOI 10.1016/j.sbi.2018.03.010
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/29625383
ISI-Number WOS:000432498100024
Document type (ISI) Journal Article, Review
 
   

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