KOPRI Repository

Structural transformation-mediated dimerization of caspase recruitment domain revealed by the crystal structure of CARD-only protein in frog virus 3

Cited 3 time in wos
Cited 3 time in scopus
Metadata Downloads
Title
Structural transformation-mediated dimerization of caspase recruitment domain revealed by the crystal structure of CARD-only protein in frog virus 3
Other Titles
CARD-only protein 의 삼차구조 규명을 통한 caspase recruitment domain 의 이량체 형성 기작연구
Authors
Kim, Chang Min
Ha, Hyun Ji
Kwon, Sunghark
Jeong, Jae-Hee
Lee, Sung Hoon
Kim, Yeon-Gil
Lee, Chang Sup
Lee, Jun Hyuck
Park, Hyun Ho
Subject
Biochemistry & Molecular Biology; Biophysics; Cell Biology
Keywords
Apoptosis; CARD-only protein; Caspase recruitment domain; Death domain superfamily; Domain swapping; crystal structure
Issue Date
2019-02
Citation
Kim, Chang Min, et al. 2019. "Structural transformation-mediated dimerization of caspase recruitment domain revealed by the crystal structure of CARD-only protein in frog virus 3". JOURNAL OF STRUCTURAL BIOLOGY, 205(2): 189-195.
Abstract
Caspase recruitment domain (CARD)-only proteins (COPs), regulate apoptosis, inflammation, and innate immunity. They inhibit the assembly of NOD-like receptor complexes such as the inflammasome and NODosome, which are molecular complexes critical for caspase-1 activation. COPs are known to interact with either caspase-1 CARD or RIP2 CARD via a CARD-CARD interaction, and inhibit caspase-1 activation or further downstream signaling. In addition to the human COPs, Pseudo-ICE, INCA, and ICEBERG, several viruses also contain viral COPs that help them escape the host immune system. To elucidate the molecular mechanism of host immunity inhibition by viral COPs, we solved the structure of a viral COP for the first time. Our structure showed that viral COP forms a structural transformation-mediated dimer, which is unique and has not been reported in any structural study of a CARD domain. Based on the current structure, and the previously solved structures of other death domain superfamily members, we propose that structural transformation-mediated dimerization might be a new strategy for dimer assembly in the death domain superfamily.
URI
https://repository.kopri.re.kr/handle/201206/10875
DOI
http://dx.doi.org/10.1016/j.jsb.2018.12.006
Appears in Collections  
2019-2019, Development of potential candidates as antibiotics based on polar genetic resources (19-19) / Lee, Jun Hyuck (PE19210)
Files in This Item

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

Browse