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Title 

Crystallization and preliminary X-ray crystallographic analysis of the PH-GRAM domain of human MTMR4

Authors 

J U LeeJ Y SonK Y YooW ShinD W ImSeung Jun KimS E RyuY S Heo

Publisher 

International Union of Crystallography

Issue Date 

2014

Citation 

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, vol. 70, no. 9, pp. 1280-1283

Keywords 

MTMR4myotubularin-related proteinsPH-GRAM domainphosphatasephosphoinositide

Abstract 

Phosphoinositide lipid molecules play critical roles in intracellular signalling pathways and are regulated by phospholipases, lipid kinases and phosphatases. In particular, phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate are related to endosomal trafficking events through the recruitment of effector proteins and are involved in the degradation step of autophagy. Myotubularin-related proteins (MTMRs) are a large family of phosphatases that catalyze the dephosphorylation of phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate at the D3 position, thereby regulating cellular phosphoinositide levels. In this study, the PH-GRAM domain of human MTMR4 was cloned, overexpressed in Escherichia coli, purified and crystallized by the vapour-diffusion method. The crystals diffracted to 3.20 ? resolution at a synchrotron beamline and belonged to either space group P61 or P65, with unit-cell parameters a = b = 109.10, c = 238.97 ?.

Citation 

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 70(9): 1280-1283

ISSN 

1744-3091

Link 

http://dx.doi.org/10.1107/S2053230X14017658

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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