ArticleActa crystallographica. Section F, Structural biology communications2014
Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed, 2 citations in OpenAlex.
- Competitive Binding of Magnesium to Calcium Binding Sites Reciprocally Regulates Transamidase and GTP Hydrolysis Activity of Transglutaminase 2.International journal of molecular sciences · 2020Article
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2 authors at 1 institution in 1 country.
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Abstract
Transglutaminase 2 (TG2) is a multi-functional protein that has been implicated in a variety of physiological cellular activities, including apoptosis, angiogenesis and cellular differentiation. Two functions of TG2 are protein cross-linking and GTP hydrolysis activities. The protein cross-linking activity of TG2 is positively controlled by calcium; however, the molecular mechanism of its Ca(2+)-dependent activity is completely unknown. In the present study, full-length human TG2 in complex with Ca(2+) was overexpressed, purified and crystallized at 20°C as a first step towards elucidating this mechanism. X-ray diffraction data were collected to a resolution of 3.4 Å from a crystal belonging to space group C2221, with unit-cell parameters a = 133.08, b = 216.30, c = 166.26 Å. Based on these data, the asymmetric unit was estimated to contain three molecules.
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