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Crystallization and preliminary X‐ray crystallographic analysis of the CARD domain of apoptosis repressor with CARD (ARC)
Author(s) -
Kim Seong Hyun,
Park Hyun Ho
Publication year - 2015
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14026211
Subject(s) - arc (geometry) , crystallization , domain (mathematical analysis) , crystallography , repressor , x ray , materials science , chemistry , physics , optics , geometry , mathematics , gene , mathematical analysis , biochemistry , organic chemistry , transcription factor
Apoptosis repressor with caspase‐recruiting domain (ARC) is an apoptosis repressor that inhibits both intrinsic and extrinsic apoptosis signalling. Human ARC contains an N‐terminal caspase‐recruiting domain (CARD domain) and a C‐terminal proline‐ and glutamic acid‐rich (P/E‐rich) domain. The CARD domain in ARC is the domain that is directly involved in inhibition of the extrinsic pathway. In this study, the N‐terminal CARD domain of ARC was overexpressed, purified and crystallized. X‐ray diffraction data were collected to a resolution of 2.1 Å and the crystals were found to belong to space group P 6 1 or P 6 5 , with unit‐cell parameters a = 98.28, b = 98.28, c = 51.86 Å, α = 90, β = 90, γ = 120°.