| Inositol polyphosphate kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the Inositol 1,4,5-trisphosphate 3-kinase A protein. | |||||||||
| Identifiers | |||||||||
| Symbol | IPK | ||||||||
| Pfam | PF03770 | ||||||||
| InterPro | IPR005522 | ||||||||
| SCOP2 | 1tzd / SCOPe / SUPFAM | ||||||||
| |||||||||
Inositol polyphosphate kinase (IPK) is a family of enzymes that have a similar 3-dimensional structure. All members of the family catalyze the transfer of phosphate groups from ATP to various inositol phosphates. Members of the family include inositol-polyphosphate multikinases, inositol-hexakisphosphate kinases, inositol-trisphosphate 3-kinases, and inositol-pentakisphosphate 2-kinase, which is more distantly related to the others
The discovery of the IPK family occurred in 1999, when a combination of biochemistry, sequence analysis, and genetics led to the classification of a family of inositol polyphosphate kinases. In 2005, the first crystal structures of an IPK family protein were published for ITPKA.
Subsequently, structures of the inositol polyphosphate multikinase and various IP6 kinases have expanded our structural understanding for how each enzyme catalyzes its specific reaction(s).
References
- "Kinase Family IPK - WikiKinome". kinase.com.
- "InterPro".
- González B, Baños-Sanz JI, Villate M, Brearley CA, Sanz-Aparicio J (2010). "Inositol 1,3,4,5,6-pentakisphosphate 2-kinase is a distant IPK member with a singular inositide binding site for axial 2-OH recognition". Proc Natl Acad Sci U S A. 107 (21): 9608–13. Bibcode:2010PNAS..107.9608G. doi:10.1073/pnas.0912979107. PMC 2906834. PMID 20453199.
- Saiardi A, Erdjument-Bromage H, Snowman AM, Tempst P, Snyder SH (1999). "Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases". Curr Biol. 9 (22): 1323–6. doi:10.1016/s0960-9822(00)80055-x. PMID 10574768.
- Odom AR, Stahlberg A, Wente SR, York JD (2000). "A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control". Science. 287 (5460): 2026–9. Bibcode:2000Sci...287.2026O. doi:10.1126/science.287.5460.2026. PMID 10720331.
- González B, Schell MJ, Letcher AJ, Veprintsev DB, Irvine RF, Williams RL (2004). "Structure of a human inositol 1,4,5-trisphosphate 3-kinase: substrate binding reveals why it is not a phosphoinositide 3-kinase". Mol Cell. 15 (5): 689–701. doi:10.1016/j.molcel.2004.08.004. PMID 15350214.
- Miller GJ, Hurley JH (2004). "Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase". Mol Cell. 15 (5): 703–11. doi:10.1016/j.molcel.2004.08.005. PMID 15350215.