Projects / Programmes source: ARIS

Structural studies of inositol polyphosphate kinases

Research activity

Code Science Field Subfield
4.06.00  Biotechnical sciences  Biotechnology   

Code Science Field
P004  Natural sciences and mathematics  Biochemistry, Metabolism 
P310  Natural sciences and mathematics  Proteins, enzymology 
P250  Natural sciences and mathematics  Condensed matter: structure, thermal and mechanical properties, crystallography, phase equilibria 
T490  Technological sciences  Biotechnology 
inositol-phosphate, kinase, crystal structure, X-ray crystallography, phosphorilation, enzymatic versatility, enzymatic specificity
Evaluation (rules)
source: COBISS
Researchers (5)
no. Code Name and surname Research area Role Period No. of publicationsNo. of publications
1.  25530  PhD Petra Draškovič  Biochemistry and molecular biology  Junior researcher  2006 - 2007  59 
2.  06108  PhD Vladimira Gaberc-Porekar  Biotechnology  Researcher  2004 - 2007  220 
3.  06135  PhD Radovan Komel  Biochemistry and molecular biology  Mentor to junior researcher  2004 - 2007  1,053 
4.  23123  MSc Tatjana Milunović  Biotechnology  Researcher  2004 - 2007  28 
5.  12048  PhD Marjetka Podobnik  Biochemistry and molecular biology  Head  2004 - 2007  313 
Organisations (1)
no. Code Research organisation City Registration number No. of publicationsNo. of publications
1.  0104  National Institute of Chemistry  Ljubljana  5051592000  21,377 
A multiplicity of inositol phosphates exists in biology, with functions in many diverse aspects of cell biology, such as ion channel physiology, membrane dynamics and nuclear signaling. This diversity involves a whole array of proteins that either metabolize inositol phosphates or mediate their intracellular functions. Recently, a family of inositol phosphate kinases was identified whose members are conserved from yeast to humans. Some of these kinases are highly specific for their substrates, and on the other hand there are inositol phosphate kinases that phosphorylate a wide array of substrates. What is the structural basis for this contrasting situation. Three-dimensional structures of the inositol phosphate kinases are not known yet and their primary structures show no significant similarity to the well studied protein kinases or phosphoinositide kinases. It is believed that different substrates can bind to the same protein in a limited number of the binding modes. These binding modes must have recognition elements which are common both in nature (phosphate and hydroxyl groups) and orientation around the inositol ring in each of these modes. This mandatory substrate recognition features are proposed to act in concert with certain other groups that define substrate recognition in a mode-specific manner. The aim of the presented proposal is to study the versatility of the inositol phosphate kinases and their substrates using X-ray crystallography as the main technique. As a model system, we will study the structures of inositol hexakisphosphate kinase (InsP6K) and inositol phosphate multikinase (IPMK) alone and with their substrates. It is expected that these structures will help us understand and explain the complexity of the inositol phosphate metabolism. Additionally, we hope that the insight into the structural basis of the inositol phosphate turn-over will contribute to development of the knowledge about the biological functions of the inositol phosphates, especially inositol pyrophosphates.
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