Roles of the valine clusters in domain 3 of the hemolytic lectin CEL-III in its oligomerization and hemolytic abilities.
The hemolytic lectin CEL-III and its site-directed mutants were expressed in Escherichia coli cells. Replacement of the valine clusters in domain 3 with alanine residues led to increased self-oligomerization in solution and higher hemolytic activity. The results suggest the involvement of these valine clusters in CEL-III oligomerization and hemolytic activity.
Department of Applied Chemistry, Faculty of Engineering, Nagasaki University, Bunkyo-machi 1-14, Nagasaki 852-8521, Japan.
Keigo
K
Hisamatsu
Hideaki
H
Unno
Shuichiro
S
Goda
Tomomitsu
T
Hatakeyama
D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D000818:Animals; D002942:Circular Dichroism; D006461:Hemolysis / Q000502:physiology*; D037102:Lectins / Q000737:chemistry*; D008969:Molecular Sequence Data; D055503:Protein Multimerization / Q000187:drug effects*; D011817:Rabbits; D014633:Valine / Q000235:genetics* / Q000502:physiology
C402644:CEL-III lectin, Cucumaria echinata; D037102:Lectins; D014633:Valine