Ontology highlight
ABSTRACT:
SUBMITTER: Jiang R
PROVIDER: S-EPMC3186399 | biostudies-literature | 2011 Oct
REPOSITORIES: biostudies-literature
Jiang Rui R Zhang Bing B Kurokawa Kenji K So Young-In YI Kim Eun-Hye EH Hwang Hyun Ok HO Lee Joon-Hee JH Shiratsuchi Akiko A Zhang Jinghai J Nakanishi Yoshinobu Y Lee Hee-Seung HS Lee Bok Luel BL
The Journal of biological chemistry 20110823 40
Serpins are protease inhibitors that play essential roles in the down-regulation of extracellular proteolytic cascades. The core serpin domain is highly conserved, and typical serpins are encoded with a molecular size of 35-50 kDa. Here, we describe a novel 93-kDa protein that contains two complete, tandemly arrayed serpin domains. This twin serpin, SPN93, was isolated from the larval hemolymph of the large beetle Tenebrio molitor. The N-terminal serpin domain of SPN93 forms a covalent complex w ...[more]