Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III. Issue 10 (2nd October 2016)

• Record Type: Journal Article
• Authors: Nagao, Tomonao; Masaki, Risa; Unno, Hideaki; Goda, Shuichiro; Hatakeyama, Tomomitsu
• Is Part Of: Bioscience, biotechnology, and biochemistry. Volume 80:Issue 10(2016)
• Page Start: 1966
• Page End: 1969
• Publication Date: 2016-10-02
• Subjects: hemolysin -- sea cucumber -- lectin -- pore-forming protein -- site-directed mutagenesis; Biotechnology -- Periodicals; Biochemistry -- Periodicals; 660.6
• DOI: 10.1080/09168451.2016.1176520
• Languages: English
• ISSNs: 0916-8451

Abstract

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.