Crystal structure of human POP1 and its distinct structural feature for PYD domain

Title
Crystal structure of human POP1 and its distinct structural feature for PYD domain
Author(s)
박현호최재영김창민서은경바트아메드에이자즈장태호이준혁[이준혁]
Keywords
PYRIN DOMAIN; 3-DIMENSIONAL STRUCTURE; EFFECTOR-DOMAIN; NMR STRUCTURE; ONLY PROTEIN; INFLAMMASOME; APOPTOSIS; CASPASE-1; MECHANISM; IMMUNITY
Issue Date
201505
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.460, no.4, pp.957 - 963
Abstract
Inflammatory caspases, such as caspase-1, which is critical for the innate immune response, are activated upon the formation of a molecular complex called the inflammasome. The inflammasome is composed of three proteins, the Nod-like receptor (NLRP, NLRC or AIM2), apoptosis associated speck-loke protein containing a caspase-recruitment domain (ASC), and caspase-1. ASC is an adaptor molecule that contains an N-terminal PYD domain and a C-terminal CARD domain for interaction with other proteins. Upon activation, the N-terminal PYD of ASC homotypically interacts with the PYD domain of the Nod-like receptor, while its C-terminal CARD homotypically interacts with the CARD domain of caspase-1. PYD only protein I (POP1) negatively regulates inflammatory response by blocking the formation of the inflammasome. POP1 directly binds to ASC via a PYD:PYD interaction, thereby preventing ASC recruitment to Nod-like receptor NLRPs. POP1-mediated regulation of inflammation is of great biological importance. Here, we report the crystal structure of human POP1 and speculate about the inhibitory mechanism of POP1-mediated inflammasome formation based on the current structure. (C) 2015 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/32547http://dx.doi.org/10.1016/j.bbrc.2015.03.134
ISSN
0006-291X
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이과대학 > 화학생화학부 > Articles
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