General interaction mode of CIDE: CIDE complex revealed by a mutation study of the Drep2 CIDE domain

Title
General interaction mode of CIDE: CIDE complex revealed by a mutation study of the Drep2 CIDE domain
Author(s)
박현호이승미
Keywords
CASPASE-ACTIVATED DNASE; APOPTOSIS-INDUCING FACTOR; DROSOPHILA-MELANOGASTER; HETERODIMERIC PROTEIN; FRAGMENTATION; ICAD; INHIBITOR; HOMOLOGY; CAD
Issue Date
201304
Publisher
ELSEVIER SCIENCE BV
Citation
FEBS LETTERS, v.587, no.7, pp.854 - 859
Abstract
The CIDE domain is a well known protein-protein interaction module that is initially detected at the apoptotic DNA fragmentation factor (DFF40/45). The interaction mechanism via the CIDE domain is not well understood. To elucidate CIDE domain mediated interactions in the apoptotic DNA fragmentation system, we conducted biochemical and mutational studies and found that the surface of CIDE domains can be divided into an acidic side and a basic side. In addition, a mutagenesis study revealed that the basic surface side of Drep2 CIDE is involved in the interaction with the acidic surface side of Drep1 CIDE and Drep3 CIDE. Our research supports the idea that a charge-charge interaction might be the general interaction mode of the CIDE: CIDE interaction. Structured summary of protein interactions: Drep2 and Drep2 bind by molecular sieving (View Interaction: 1, 2) Drep1 and Drep2 bind by molecular sieving (View interaction) Drep3 and Drep2 bind by molecular sieving (View interaction) Drep2 and Drep3 bind by blue native page (View interaction) Drep2 and Drep1 bind by blue native page (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/26044http://dx.doi.org/10.1016/j.febslet.2013.02.031
ISSN
0014-5793
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이과대학 > 화학생화학부 > Articles
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