Effects of amino acid mutations in the pore-forming domain of the hemolytic lectin CEL-III.
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.
a Biomolecular Chemistry Laboratory, Graduate School of Engineering , Nagasaki University , Nagasaki , Japan.
Tomonao
T
Nagao
a Biomolecular Chemistry Laboratory, Graduate School of Engineering , Nagasaki University , Nagasaki , Japan.
Risa
R
Masaki
a Biomolecular Chemistry Laboratory, Graduate School of Engineering , Nagasaki University , Nagasaki , Japan.
Hideaki
H
Unno
a Biomolecular Chemistry Laboratory, Graduate School of Engineering , Nagasaki University , Nagasaki , Japan.
Shuichiro
S
Goda
a Biomolecular Chemistry Laboratory, Graduate School of Engineering , Nagasaki University , Nagasaki , Japan.
Tomomitsu
T
Hatakeyama
D037102:Lectins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D016062:Porosity; D000072757:Protein Conformation, beta-Strand; D000072417:Protein Domains
C402644:CEL-III lectin, Cucumaria echinata; D037102:Lectins
hemolysin; lectin; pore-forming protein; sea cucumber; site-directed mutagenesis