Ontology highlight
ABSTRACT:
SUBMITTER: Jia N
PROVIDER: S-EPMC5290818 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Jia Ning N Liu Nan N Cheng Wang W Jiang Yong-Liang YL Sun Hui H Chen Lan-Lan LL Peng Junhui J Zhang Yonghui Y Ding Yue-He YH Zhang Zhi-Hui ZH Wang Xuejuan X Cai Gang G Wang Junfeng J Dong Meng-Qiu MQ Zhang Zhiyong Z Wu Hui H Wang Hong-Wei HW Chen Yuxing Y Zhou Cong-Zhao CZ
EMBO reports 20151228 2
Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, the mechanism of receptor recognition and/or pore formation of the eukaryotic members remains unknown. Here, we present the first crystal and electron microscopy structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a β-prism lectin module followed by an aerolysin module. Specific binding of the l ...[more]