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.
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