STRUCTURAL AND FUNCTIONAL DIVERSITY OF PHOSPHOINOSITIDE 3-KINASES

Citation
Mj. Zvelebil et al., STRUCTURAL AND FUNCTIONAL DIVERSITY OF PHOSPHOINOSITIDE 3-KINASES, Philosophical transactions-Royal Society of London. Biological sciences, 351(1336), 1996, pp. 217-223
Citations number
50
Categorie Soggetti
Biology
ISSN journal
09628436
Volume
351
Issue
1336
Year of publication
1996
Pages
217 - 223
Database
ISI
SICI code
0962-8436(1996)351:1336<217:SAFDOP>2.0.ZU;2-Z
Abstract
Phosphoinositide 3-kinases (PI3-kinases) have been shown to be recruit ed to cell surface receptor signal complexes whose formation is trigge red by growth factors, cytokines and other ligands. PI3-kinases are al so involved in protein sorting phenomena. A number of PI3-kinase isoty pes have been characterised in several laboratories. Here the relation s between the PI3-kinases, PI4-kinases and PI5-kinases and other poten tial phosphoinositide kinases are analysed. A study of the relation of structure to function for sequence motifs defined through the use of homology searches and protein modelling techniques is described and us ed to assign the family of phosphoinositide kinases to subgroups.