Cloning of a pore-forming subunit of ATP-sensitive potassium channel from Clonorchis sinensis | Zendy

Seung-Young Hwang | Zendy; HyeJin Han | Zendy; Sohee Kim | Zendy; Sae-Gwang Park | Zendy; DaeHyun Seog | Zendy; Nari Kim | Zendy; Jin Han | Zendy; JoonYong Chung | Zendy; Weon-Gyu Kho | Zendy

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Cloning of a pore-forming subunit of ATP-sensitive potassium channel from Clonorchis sinensis

Author(s) -

Seung-Young Hwang,

HyeJin Han,

Sohee Kim,

Sae-Gwang Park,

DaeHyun Seog,

Nari Kim,

Jin Han,

JoonYong Chung,

Weon-Gyu Kho

Publication year - 2003

Publication title -

korean journal of parasitology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.555

H-Index - 42

eISSN - 1738-0006

pISSN - 0023-4001

DOI - 10.3347/kjp.2003.41.2.129

Subject(s) - complementary dna , clonorchis sinensis , open reading frame , peptide sequence , amino acid , biology , protein subunit , potassium channel , cloning (programming) , microbiology and biotechnology , cdna library , sequence analysis , gene , biochemistry , biophysics , zoology , computer science , helminths , programming language

A complete cDNA sequence encoding a pore-forming subunit (Kir6.2) of ATP-sensitive potassium channel in the adult worm, Clonorchis sinensis, termed CsKir6.2, was isolated from an adult cDNA library. The cDNA contained a single open-reading frame of 333 amino acids, which has a structural motif (a GFG-motif) of the putative pore-forming loop of the Kir6.2. Peculiarly, the CsKir6.2 shows a lack-sequence structure, which deleted 57 amino acids were deleted from its N-terminus. The predicted amino acid sequence revealed a highly conserved sequence as other known other Kir6.2 subunits. The mRNA was weekly expressed in the adult worm.

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