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Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III


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Title: Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III
Authors: Nagao, Tomonao / Masaki, Risa / Unno, Hideaki / Goda, Shuichiro / Hatakeyama, Tomomitsu
Issue Date: 22-Apr-2016
Publisher: 日本農芸化学会 / Japan Society for Bioscience, Biotechnology, and Agrochemistry
Citation: Bioscience, Biotechnology, and Biochemistry, 80(10), pp.1966-1969; 2016
Abstract: The hemolytic lectin CEL-III forms transmembrane pores in the membranes of target cells. A study on the effect of site-directed mutation at Lys405 in domain 3 of CEL-III indicated that replacements of this residue by relatively smaller residues lead to a marked increase in hemolytic activity, suggesting that moderately destabilizing domain 3 facilitates formation of transmembrane pores through conformational changes.
Keywords: Hemolysin / Lectin / Pore-forming protein / Sea cucumber / Site-directed mutagenesis
URI: http://hdl.handle.net/10069/37281
ISSN: 09168451
DOI: 10.1080/09168451.2016.1176520
Rights: © 2016 Japan Society for Bioscience, Biotechnology, and Agrochemistry.
Type: Journal Article
Text Version: author
Appears in Collections:Articles in academic journal

Citable URI : http://hdl.handle.net/10069/37281

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