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Title 

Expression, purification, crystallization and preliminary crystallographic analysis of human myotubularin-related protein 3

Authors 

J Y SonJ U LeeK 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. 1240-1243

Keywords 

MTMR3myotubularin-related proteinsPH-GRAM domainphosphatasephosphoinositide

Abstract 

Myotubularin-related proteins are a large family of phosphatases that have the catalytic activity of dephosphorylating the phospholipid molecules phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate. Each of the 14 family members contains a phosphatase catalytic domain, which is inactive in six family members owing to amino-acid changes in a key motif for the activity. All of the members also bear PH-GRAM domains, which have low homologies between them and have roles that are not yet clear. Here, the cloning, expression, purification and crystallization of human myotubularin-related protein 3 encompassing the PH-GRAM and the phosphatase catalytic domain are reported. Preliminary X-ray crystallographic analysis shows that the crystals diffracted to 3.30 ? resolution at a synchrotron X-ray source. The crystals belonged to space group C2, with unit-cell parameters a = 323.3, b = 263.3, c = 149.4 ?, β = 109.7°.

Citation 

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications, 70(9): 1240-1243

ISSN 

1744-3091

Link 

http://dx.doi.org/10.1107/S2053230X14015714

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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