Structural basis of six bladed beta propeller lectins AAL and RSL

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Authors	KOSTLÁNOVÁ Nikola MITCHELL Edward IMBERTY Anne WIMMEROVÁ Michaela
Year of publication	2007
Type	Article in Proceedings
Conference	Materials and Structure in Chemistry, Biology,Physics and Technology
MU Faculty or unit	Faculty of Science
Citation
Field	Biochemistry
Keywords	lectin;beta propeller; AAL; RSL;
Description	This contribution describes two fucose binding lectins: AAL (312 amino acids), the fungal lectin from Aleuria aurentia, and RSL (90 amino acids),the bacterial lectin from Ralstonia solanacearum. The crystal structure of AAL, the first structure of fungal lectin, was found to be a six bladed beta propeller with a small antiparallel two stranded beta sheet that plays a role in dimerization.The RSL monomer is composed of two four stranded beta sheets and assembles as a trimer, forming six bladed beta propeller fold very similar to that of AAL.
Related projects:	Proteins in metabolism and interaction of organisms with the environment Biomolecular centre