Access the full text.
Sign up today, get DeepDyve free for 14 days.
Loading next page...
/lp/wiley/cloning-expression-purification-crystallization-and-x-ray-analysis-of-x0KQP8Pre1
References (19)
-
R. Gill, F. Mohammed, R. Badyal, L. Coates, P. Erskine, D. Thompson, J. Cooper, M. Gore, S. Wood
Biological Crystallography High-resolution Structure of Myo-inositol Monophosphatase, the Putative Target of Lithium Therapy -
P. Emsley, B. Lohkamp, William Scott, K. Cowtan (2010)
Features and development of CootActa Crystallographica Section D: Biological Crystallography, 66
-
Liangjing Chen, M. Roberts (1998)
Cloning and Expression of the Inositol Monophosphatase Gene from Methanococcus jannaschii and Characterization of the EnzymeApplied and Environmental Microbiology, 64
-
P. Evans (2006)
Scaling and assessment of data quality.Acta crystallographica. Section D, Biological crystallography, 62 Pt 1
-
Loretta HallcherS, W. Sherman (1980)
The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain.The Journal of biological chemistry, 255 22
-
N. Gee, C. Ragan, Keith Watling, S. Aspley, R. Jackson, G. Reid, David GANIt, Janis SHUTEt (1988)
The purification and properties of myo-inositol monophosphatase from bovine brain.The Biochemical journal, 249 3
-
T. Battye, Luke Kontogiannis, O. Johnson, H. Powell, A. Leslie (2011)
iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLMActa Crystallographica Section D: Biological Crystallography, 67
-
G. Mcallister, P. Whiting, E. Hammond, M. Knowles, J. Atack, Fred Bailey, R. Maigetter, C. Ragan, Merck (1992)
cDNA cloning of human and rat brain myo-inositol monophosphatase. Expression and characterization of the human recombinant enzyme.The Biochemical journal, 284 ( Pt 3)
-
A. Mccoy, R. Grosse-Kunstleve, P. Adams, M. Winn, L. Storoni, R. Read (2007)
Phaser crystallographic softwareJournal of Applied Crystallography, 40
-
R. Saiki, D. Gelfand, S. Stoffel, S. Scharf, R. Higuchi, G. Horn, K. Mullis, H. Erlich (1988)
Primer-directed enzymatic amplification of DNA with a thermostable DNA polymerase.Science, 239 4839
-
G. Gillaspy, J. Keddie, K. Oda, W. Gruissem (1995)
Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a multigene family.The Plant cell, 7
-
Smith (1985)
10.1016/0003-2697(85)90442-7Anal. Biochem., 150
-
S. Pollack, J. Atack, M. Knowles, G. Mcallister, C. Ragan, R. Baker, S. Fletcher, L. Iversen, H. Broughton (1994)
Mechanism of inositol monophosphatase, the putative target of lithium therapy.Proceedings of the National Academy of Sciences of the United States of America, 91 13
-
R. Bone, J. Springer, J. Atack (1992)
Structure of inositol monophosphatase, the putative target of lithium therapy.Proceedings of the National Academy of Sciences of the United States of America, 89 21
-
J. Atack, Susan Cook, A. Watt, S. Fletcher, C. Ragan (1993)
In Vitro and In Vivo Inhibition of Inositol Monophosphatase by the Bisphosphonate L‐690,330Journal of Neurochemistry, 60
-
K. Takimoto, M. Okada, Y. Matsuda, H. Nakagawa (1985)
Purification and properties of myo-inositol-1-phosphatase from rat brain.Journal of biochemistry, 98 2
-
K. Itaya, Michio Ui (1966)
A new micromethod for the colorimetric determination of inorganic phosphate.Clinica chimica acta; international journal of clinical chemistry, 14 3
-
Gill (2005)
10.1107/S0907444905004038Acta Cryst. D, 61
-
M. Berridge, R. Irvine (1984)
Inositol trisphosphate, a novel second messenger in cellular signal transductionNature, 312
- Publisher
- Wiley
- Copyright
- International Union of Crystallography, 2012
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309112035191
- pmid
- 23027737
- Publisher site
- See Article on Publisher Site
Abstract
Inositol monophosphatase (IMPase) catalyses the hydrolysis of inositol monophosphate to inositol and is crucial in the phosphatidylinositol (PI) signalling pathway. Lithium, which is the drug of choice for bipolar disorder, inhibits IMPase at therapeutically relevant plasma concentrations. Both mouse IMPase 1 (MmIMPase 1) and human IMPase 1 (HsIMPase 1) were cloned into pRSET5a, expressed in Escherichia coli, purified and crystallized using the sitting‐drop method. The structures were solved at resolutions of 2.4 and 1.7 Å, respectively. Comparison of MmIMPase 1 and HsIMPase 1 revealed a core r.m.s. deviation of 0.516 Å.
Journal
Acta Crystallographica Section F – Wiley
Published: Oct 1, 2012