Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Echinobase
ECB-ART-42817
Acta Crystallogr Sect F Struct Biol Cryst Commun 2013 Apr 01;69Pt 4:416-20. doi: 10.1107/S1744309113004065.
Show Gene links Show Anatomy links

Crystallization and preliminary crystallographic study of oligomers of the haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata.

Unno H , Hisamatsu K , Nagao T , Tateya Y , Matsumoto N , Goda S , Hatakeyama T .


???displayArticle.abstract???
CEL-III is a Ca(2+)-dependent haemolytic lectin isolated from the marine invertebrate Cucumaria echinata. This lectin binds to Gal/GalNAc-containing carbohydrate chains on the cell surface and, after conformational changes, oligomerizes to form ion-permeable pores in cell membranes. CEL-III also forms soluble oligomers similar to those formed in cell membranes upon binding of specific carbohydrates in high-pH and high-salt solutions. These soluble and membrane CEL-III oligomers were crystallized and X-ray diffraction data were collected. Crystals of soluble oligomers and membrane oligomers diffracted X-rays to 3.3 and 4.2 Å resolution, respectively, using synchrotron radiation and the former was found to belong to space group C2. Self-rotation functional analysis of the soluble oligomer crystal suggested that it might be composed of heptameric CEL-III.

???displayArticle.pubmedLink??? 23545649
???displayArticle.pmcLink??? PMC3614168
???displayArticle.link??? Acta Crystallogr Sect F Struct Biol Cryst Commun


Genes referenced: LOC100887844 LOC115919910

References [+] :
Araki, The complete amino acid sequence of the B-chain of ricin E isolated from small-grain castor bean seeds. Ricin E is a gene recombination product of ricin D and Ricinus communis agglutinin. 1987, Pubmed