Affiliation:
1. Biomolecular Chemistry Laboratory, Graduate School of Engineering, Nagasaki University, Nagasaki, Japan
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.
Funder
Japan Society for the Promotion of Science
Publisher
Oxford University Press (OUP)
Subject
Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology
Cited by
3 articles.
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