Q868M7Uniprot
Fold
Class
Family
Origin
Species
Available structures
Related proteins
> 50% identity
> 50% identity
PubMed
Unno H, Goda S, Hatakeyama T.
Hemolytic lectin CEL-III heptamerizes via a large structural transition from alpha-helices to a beta-barrel during the transmembrane pore formation process. The Journal of biological chemistry 2014
Hemolytic lectin CEL-III heptamerizes via a large structural transition from alpha-helices to a beta-barrel during the transmembrane pore formation process. The Journal of biological chemistry 2014
PubMed
Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, Kusunoki M
C-type lectin-like carbohydrate-recognition of the hemolytic lectin CEL-III containing ricin-type beta-trefoil folds J. Biol. Chem. 2007
C-type lectin-like carbohydrate-recognition of the hemolytic lectin CEL-III containing ricin-type beta-trefoil folds J. Biol. Chem. 2007
PubMed
Hatakeyama T, Unno H, Kouzuma Y, Uchida T, Eto S, Hidemura H, Kato N, Yonekura M, Kusunoki M
C-type lectin-like carbohydrate-recognition of the hemolytic lectin CEL-III containing ricin-type beta-trefoil folds J. Biol. Chem. 2007
C-type lectin-like carbohydrate-recognition of the hemolytic lectin CEL-III containing ricin-type beta-trefoil folds J. Biol. Chem. 2007
PubMed
Uchida T, Yamasaki T, Eto S, Sugawara H, Kurisu G, Nakagawa A, Kusunoki M, Hatakeyama T.
Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism. The Journal of biological chemistry 2004
Crystal structure of the hemolytic lectin CEL-III isolated from the marine invertebrate Cucumaria echinata: implications of domain structure for its membrane pore-formation mechanism. The Journal of biological chemistry 2004
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