Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+

Title
Crystallization and preliminary X-ray crystallographic studies of transglutaminase 2 in complex with Ca2+
Author(s)
박현호장태호
Keywords
PIG LIVER TRANSGLUTAMINASE; TISSUE TRANSGLUTAMINASE; CELL-DIFFERENTIATION; STRUCTURAL BASIS; CALCIUM-IONS; TUMOR-GROWTH; GTP; IDENTIFICATION; ANGIOGENESIS; TRIPHOSPHATE
Issue Date
201404
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, v.70, pp.513 - 516
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 Ca2+-dependent activity is completely unknown. In the present study, full-length human TG2 in complex with Ca2+ was overexpressed, purified and crystallized at 20 degrees C as a first step towards elucidating this mechanism. X-ray diffraction data were collected to a resolution of 3.4 angstrom from a crystal belonging to space group C222(1), with unit-cell parameters a = 133.08, b = 216.30, c = 166.26 angstrom. Based on these data, the asymmetric unit was estimated to contain three molecules.
URI
http://hdl.handle.net/YU.REPOSITORY/32495http://dx.doi.org/10.1107/S2053230X1400510X
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
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