• Home
  • Search Results
  • Crystal structure of human POP1 and its distinct structural feature for PYD domain.

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

Biochemical and biophysical research communications (2015-04-04)
Jae Young Choi, Chang Min Kim, Eun Kyung Seo, Eijaz Ahmed Bhat, Tae-Ho Jang, Jun Hyuck Lee, Hyun Ho Park

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 1 (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.

Product Number
Product Description

Sodium formate, 99.998% trace metals basis
Sodium formate, BioUltra, ≥99.0% (NT)