2014
DOI: 10.1107/s2053230x1400510x
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Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+

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 over… Show more

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Cited by 2 publications
(2 citation statements)
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“…To identify the Ca 2+ binding sites, a Ca 2+ -containing crystal of TG2 was produced in totally different crystallization conditions from those used for the previous structural study of TG2 [25]. A relatively low-resolution structure of 3.56 Å was solved and refined to R work = 22.5% and R free = 26.3%.…”
Section: Identification Of New Ca 2+ -Binding Sites In Tg2mentioning
confidence: 99%
See 1 more Smart Citation
“…To identify the Ca 2+ binding sites, a Ca 2+ -containing crystal of TG2 was produced in totally different crystallization conditions from those used for the previous structural study of TG2 [25]. A relatively low-resolution structure of 3.56 Å was solved and refined to R work = 22.5% and R free = 26.3%.…”
Section: Identification Of New Ca 2+ -Binding Sites In Tg2mentioning
confidence: 99%
“…The method for TG2 protein expression and purification was introduced in previous structural studies [25]. Briefly, the full-length human TG2 gene encoding G224 was inserted into a home-made pOKD5 vector.…”
Section: Protein Expression and Purificationmentioning
confidence: 99%