Crystallization and preliminary X-ray crystallographic studies of the CARD domain of human CARMA1

Title
Crystallization and preliminary X-ray crystallographic studies of the CARD domain of human CARMA1
Author(s)
박현호박진희
Keywords
NF-KAPPA-B; T-CELL-ACTIVATION; MALT LYMPHOMA; BCL10; SUPERFAMILY; UBIQUITINATION; PATHWAY; BINDING; KEY
Issue Date
201304
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.69, pp.435 - 437
Abstract
The CARMA1 signalosome, which is composed of CARMA1 [caspase recruitment domain (CARD) containing MAGUK protein 1], BCL10 (B-cell lymphoma 10) and MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1), is a molecular-signalling complex that performs pivotal functions in T-cell receptor (TCR) and B-cell receptor (BCR) mediated NF-kappa B activation. In this study, the CARD domain of human CARMA1 (CARMA1 CARD), corresponding to amino acids 14-109, was overexpressed in Escherichia coli using an engineered C-terminal His tag. CARMA1 CARD was then purified to homogeneity and crystallized at 293 K. Finally, X-ray diffraction data were collected to a resolution of 3.2 angstrom from a crystal belonging to space group P2(1)2(1)2(1) with unit-cell parameters a = 45.73, b = 53.37, c = 91.89 angstrom.
URI
http://hdl.handle.net/YU.REPOSITORY/26067http://dx.doi.org/10.1107/S1744309113005642
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
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